#ABCTransporter
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cp-trendsbiochem.bsky.social
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...
April 18, 2025 at 2:53 PM
toptags.bsky.social
🚀 BlueSky trending hashtags (15m):

#booksky #birds #photography #art #nature #birdphotography #furry #furryart #birdoftheday #gamedev #digitalart #writingcommunity #ecoli #abctransporter #cryoem
November 27, 2025 at 10:15 AM
stcmicrobeblog.bsky.social
cross·posting from 𝕏 > bacterial cell divisionists take note 👇

Structural insights into the FtsEX-EnvC complex regulation on septal PG hydrolysis in V. cholerae
www.biorxiv.org/content/10.1...
#CryoEM #ABCtransporter #MembraneProteins #MicroSky

thx @Bramkamplab for the shoutout🙏
figure from linked cit.
October 9, 2023 at 10:06 PM
flo-dimeo.bsky.social
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...
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…
www.sciencedirect.com
March 26, 2025 at 7:38 AM
plosbiology.org
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
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.
November 27, 2025 at 5:30 PM
plosbiology.org
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
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.
November 27, 2025 at 10:01 AM
plosbiology.org
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
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.
November 28, 2025 at 9:15 AM
cp-trendsparasitol.bsky.social
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...
March 22, 2025 at 7:48 AM
plosbiology.org
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
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.
November 27, 2025 at 6:03 PM
plosbiology.org
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
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.
November 27, 2025 at 2:05 PM
schwalbe-lab.bsky.social
Excited to see a new publication in Communications Biology! 🎉 Read it here: doi.org/10.1038/s420...

#SialicAcid #StreptococcusPneumoniae #ABCTransporter #CarbohydrateTransport #StructuralBiology #Microbiology
Streptococcus pneumoniae substrate binding protein SatA specifically recognises the α-anomer of N-acetylneuraminic acid - Communications Biology
The respiratory pathogen Streptococcus pneumoniae uses the substrate binding protein SatA of the ABC transporter SatBC–MsmK to specifically bind the α-anomer of N-acetylneuraminic acid, the immediate ...
doi.org
July 29, 2026 at 10:12 AM
vlamba13.bsky.social
Excited to share a new paper This research offers novel insights into the immunological function of mosquito ABC transporters and presents molecular evidence linking diverse immune stimulations to the transcriptional regulation of midgut-specific ABCtransporter genes #Mosquito#immunity rdcu.be/d8iUC
Midgut immune profiling and functional characterization of Aedes aegypti ABC transporter gene(s) using systemic and local bacterial challenges | Parasites & Vectors
rdcu.be
February 1, 2025 at 10:40 PM
plosbiology.org
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
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.
November 28, 2025 at 2:15 PM
cp-trendsparasitol.bsky.social
#microbial #metabolites #virulence #ABCtransporter @inrsciences.bsky.social @rimuhc.bsky.social @mcgill-microbiome.bsky.social
September 26, 2025 at 4:09 PM
jprnews.bsky.social
“ATP-dependent binding cassette transporter ClABCI6 promotes the expression of citrus yellow vein clearing virus via inhibiting salicylic acid pathway.” Song et al. #ABCtransporter #CitrusYellowVeinClearingVirus #SalicylicAcid　link.springer.com/article/10.1...
ATP-dependent binding cassette transporter ClABCI6 promotes the expression of citrus yellow vein clearing virus via inhibiting salicylic acid pathway - Journal of Plant Research
ATP-dependent binding cassette (ABC) transporters constitute a class of proteins that utilize ATP hydrolysis to actively transport diverse substrates across cellular membranes and play crucial roles i...
link.springer.com
May 30, 2026 at 4:19 AM
alamlab.bsky.social
Happy to share our review on Human ABC subfamily A transporters. Thank you to Biochemical Society Transactions #BiochemSocTrans for the invite. #abca #abctransporter #alzheimers #hdl #ldl #apolipoproteins #lipidtransport portlandpress.com/biochemsoctr...
Lipid transport mechanisms in human ABCA family transporters: a structural perspective
Abstract. ATP-binding cassette (ABC) transporters are essential membrane proteins that couple ATP hydrolysis to move diverse substrates across lipid bilayers through large-scale conformational changes...
portlandpress.com
May 7, 2026 at 8:55 PM
alamlab.bsky.social
#ABCA #ABCA7 #ABCtransporter #Alzheimers
February 15, 2025 at 1:39 PM
flo-dimeo.bsky.social
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...
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...
doi.org
March 3, 2025 at 7:26 AM