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#ABCtransporter

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Posts tagged #ABCtransporter

ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

This Primer explores a @plosbiology.org study that reports #cryoEM structures of the #Ecoli Type VII #ABCtransporter system YbbAP-TesA, suggesting that YbbAP extracts hydrophobic compounds from the bacterial inner membrane 🧪 Paper: plos.io/49EhNHD Primer: plos.io/48ndzSq

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ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

This Primer explores a @plosbiology.org study that reports #cryoEM structures of the #Ecoli Type VII #ABCtransporter system YbbAP-TesA, suggesting that YbbAP extracts hydrophobic compounds from the bacterial inner membrane 🧪 Paper: plos.io/49EhNHD Primer: plos.io/48ndzSq

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ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

ABC transporters and the recruitment of a distal enzyme activity. Top left: a simplified schematic of the conventional ABC transporters, posited to switch between inward- and outward-facing states. ATP binding and hydrolysis drives the conformational switch and resetting the system. Bottom left: a schematic for the group that communicate conformational changes across the membrane, but do not form channels to displace transport substrates. Right: this schematic depicts the action of the system studied by McAndrew and colleagues, where the conformational propagation helps to deliver substrates to a captive and orientated enzyme—in this case, a hydrolytic esterase.

This Primer explores a @plosbiology.org study that reports #cryoEM structures of the #Ecoli Type VII #ABCtransporter system YbbAP-TesA, suggesting that YbbAP extracts hydrophobic compounds from the bacterial inner membrane 🧪 Paper: plos.io/49EhNHD Primer: plos.io/48ndzSq

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Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom:  Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom: Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Structures of 3 of the 4 #Ecoli Type VII #ABCtransporter systems are known. @allistercrow.bsky.social &co use #cryoEM structures to show that the 4th, YbbAP, may extract hydrophobic compounds from the inner membrane & present them to periplasmic TesA for hydrolysis @plosbiology.org 🧪 plos.io/49EhNHD

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Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom:  Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom: Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Structures of 3 of the 4 #Ecoli Type VII #ABCtransporter systems are known. @allistercrow.bsky.social &co use #cryoEM structures to show that the 4th, YbbAP, may extract hydrophobic compounds from the inner membrane & present them to periplasmic TesA for hydrolysis @plosbiology.org 🧪 plos.io/49EhNHD

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🚀 BlueSky trending hashtags (15m):

#booksky #birds #photography #art #nature #birdphotography #furry #furryart #birdoftheday #gamedev #digitalart #writingcommunity #ecoli #abctransporter #cryoem

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Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom:  Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Top left: CryoEM map for the ATP-bound YbbAP at 3.6 Å resolution, and (below)ATP-bound YbbAP-TesA complex contoured to visualize the detergent belt. Maps are shown at two contour levels—a partially transparent low contour map is shown in white (4.5 σ), and a high contour map is shown colored by nearest protein chain (7 σ). Top right: Structures of apo YbbAP, ATP analogue-bound YbbAP, and ATP analogue-bound YbbAP-TesA. Proteins are shown in cartoon representation (YbbA green, YbbP teal, and TesA pink), and the non-hydrolyzable ATP analogue (AMP-PNP) is shown in blue atomic spheres. Bottom: Biological functions of the four Type VII ABC transporters in Escherichia coli. From left to right: YbbAP-TesA forms a novel type VII ABC transporter involved in extraction of hydrophobic compounds from the inner membrane and enzymatic hydrolysis in the periplasm; FtsEX-EnvC uses transmembrane conformational changes to regulate the activity of peptidoglycan amidases in the periplasm; MacAB-TolC drive efflux of antibiotics and small toxins across the outer membrane; and LolCDE extracts lipoproteins from the inner membrane and delivers them to the outer membrane via the LolA shuttle.

Structures of 3 of the 4 #Ecoli Type VII #ABCtransporter systems are known. @allistercrow.bsky.social &co use #cryoEM structures to show that the 4th, YbbAP, may extract hydrophobic compounds from the inner membrane & present them to periplasmic TesA for hydrolysis @plosbiology.org 🧪 plos.io/49EhNHD

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#microbial #metabolites #virulence #ABCtransporter @inrsciences.bsky.social @rimuhc.bsky.social @mcgill-microbiome.bsky.social

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Now online - the Review "Plant steroids on the move: mechanisms of #brassinosteroid export" from @jennyrussinova.bsky.social and co.

#PlantHormones #ABCTransporter #ABCB19 #ABCB1

Read it here: authors.elsevier.com/a/1kx%7Ex3S6...

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Membrane-dependent dynamics and dual translocation mechanisms of ABCB4: Insights from molecular dynamics simulations ABCB4 is an ATP-binding cassette transporter expressed at the canalicular membrane of hepatocytes and responsible for translocating phosphatidylcholin…

Veronica's work about structural dynamics of ABCB4 finally out in CSBJ @insermna.bsky.social @inserm.fr #ABCtransporter #MD #membprot #compchem www.sciencedirect.com/science/arti...

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Drs James Westwood & Sukhmanpreet Kaur highlight Jiayang Li, Qi Xie, Feifei Yu & colleagues’ recent @cp-cell.bsky.social article on suppressing #strigolactone #exudation hides the host from a parasitic plant. #Striga #Witchweed #ABCtransporter #Germination

authors.elsevier.com/a/1koWQ5Eb1x...

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Membrane-Dependent Dynamics and Dual Translocation Mechanisms of ABCB4: Insights from Molecular Dynamics Simulations ABCB4 is an ATP-binding cassette transporter expressed at the canalicular membrane of hepatocytes and responsible for translocating phosphatidylcholine into bile. Despite the recent cryo-EM structures...

Happy to share here our revised version of our study about membrane-dependent structural dynamics of ABCB4 membrane transporter. Huge work from Veronica @inserm.fr @insermna.bsky.social @unilim.bsky.social #ABCtransporter #MD doi.org/10.1101/2024...

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#ABCA #ABCA7 #ABCtransporter #Alzheimers

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