7ekm: Difference between revisions
New page: '''Unreleased structure''' The entry 7ekm is ON HOLD Authors: Zhang, S.S. Description: mitochondrial outer membrane protein Category: Unreleased Structures Category: Zhang, S.S |
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==Mitochondrial outer membrane protein== | |||
<StructureSection load='7ekm' size='340' side='right'caption='[[7ekm]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EKM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ekm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ekm OCA], [https://pdbe.org/7ekm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ekm RCSB], [https://www.ebi.ac.uk/pdbsum/7ekm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ekm ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ABCB6 plays a crucial role in energy-dependent porphyrin transport, drug resistance, toxic metal resistance, porphyrin biosynthesis, protection against stress, and encoding a blood group system Langereis antigen. However, the mechanism underlying porphyrin transport is still unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structures of nanodisc-reconstituted human ABCB6 trapped in an apo-state and an ATP-bound state at resolutions of 3.6 and 3.5 A, respectively. Our structures reveal a unique loop in the transmembrane domain (TMD) of ABCB6, which divides the TMD into two cavities. It restrains the access of substrates in the inward-facing state and is removed by ATP-driven conformational change. No ligand cavities were observed in the nucleotide-bound state, indicating a state following substrate release but prior to ATP hydrolysis. Structural analyses and functional characterizations suggest an "ATP-switch" model and further reveal the conformational changes of the substrate-binding pockets triggered by the ATP-driven regulation. | |||
Molecular insights into the human ABCB6 transporter.,Song G, Zhang S, Tian M, Zhang L, Guo R, Zhuo W, Yang M Cell Discov. 2021 Jul 27;7(1):55. doi: 10.1038/s41421-021-00284-z. PMID:34312373<ref>PMID:34312373</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Zhang | <div class="pdbe-citations 7ekm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ABC transporter 3D structures|ABC transporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Zhang SS]] | |||
Latest revision as of 08:44, 5 June 2024
Mitochondrial outer membrane proteinMitochondrial outer membrane protein
Structural highlights
Publication Abstract from PubMedABCB6 plays a crucial role in energy-dependent porphyrin transport, drug resistance, toxic metal resistance, porphyrin biosynthesis, protection against stress, and encoding a blood group system Langereis antigen. However, the mechanism underlying porphyrin transport is still unclear. Here, we determined the cryo-electron microscopy (cryo-EM) structures of nanodisc-reconstituted human ABCB6 trapped in an apo-state and an ATP-bound state at resolutions of 3.6 and 3.5 A, respectively. Our structures reveal a unique loop in the transmembrane domain (TMD) of ABCB6, which divides the TMD into two cavities. It restrains the access of substrates in the inward-facing state and is removed by ATP-driven conformational change. No ligand cavities were observed in the nucleotide-bound state, indicating a state following substrate release but prior to ATP hydrolysis. Structural analyses and functional characterizations suggest an "ATP-switch" model and further reveal the conformational changes of the substrate-binding pockets triggered by the ATP-driven regulation. Molecular insights into the human ABCB6 transporter.,Song G, Zhang S, Tian M, Zhang L, Guo R, Zhuo W, Yang M Cell Discov. 2021 Jul 27;7(1):55. doi: 10.1038/s41421-021-00284-z. PMID:34312373[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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