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7s9z
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7s9z is ON HOLD Authors: Mendez, D.L., Lowder, E.P., Tillman, D.E., Sutherland, M.C., Collier, A.L., Rau, M.J., Fitzpatrick, J.A., Kranz, R.G. Desc...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Helicobacter Hepaticus CcsBA Closed Conformation== | |
| + | <StructureSection load='7s9z' size='340' side='right'caption='[[7s9z]], [[Resolution|resolution]] 4.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7s9z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S9Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEB:HEME+B/C'>HEB</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></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=7s9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s9z OCA], [https://pdbe.org/7s9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s9z RCSB], [https://www.ebi.ac.uk/pdbsum/7s9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s9z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Although the individual structures and respiratory functions of cytochromes are well studied, the structural basis for their assembly, including transport of heme for attachment, are unknown. We describe cryo-electron microscopy (cryo-EM) structures of CcsBA, a bifunctional heme transporter and cytochrome c (cyt c) synthase. Models built from the cryo-EM densities show that CcsBA is trapped with heme in two conformations, herein termed the closed and open states. The closed state has heme located solely at a transmembrane (TM) site, with a large periplasmic domain oriented such that access of heme to the cytochrome acceptor is denied. The open conformation contains two heme moieties, one in the TM-heme site and another in an external site (P-heme site). The presence of heme in the periplasmic site at the base of a chamber induces a large conformational shift that exposes the heme for reaction with apocytochrome c (apocyt c). Consistent with these structures, in vivo and in vitro cyt c synthase studies suggest a mechanism for transfer of the periplasmic heme to cytochrome. | ||
| - | + | Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.,Mendez DL, Lowder EP, Tillman DE, Sutherland MC, Collier AL, Rau MJ, Fitzpatrick JAJ, Kranz RG Nat Chem Biol. 2022 Jan;18(1):101-108. doi: 10.1038/s41589-021-00935-y. Epub 2021, Dec 20. PMID:34931065<ref>PMID:34931065</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7s9z" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Sutherland, M | + | [[Category: Collier, A L]] |
| - | [[Category: Tillman, D | + | [[Category: Fitzpatrick, J A]] |
| + | [[Category: Kranz, R G]] | ||
| + | [[Category: Lowder, E P]] | ||
| + | [[Category: Mendez, D L]] | ||
| + | [[Category: Rau, M J]] | ||
| + | [[Category: Sutherland, M C]] | ||
| + | [[Category: Tillman, D E]] | ||
| + | [[Category: Cytochrome c biogenesis]] | ||
| + | [[Category: Heme lyase]] | ||
| + | [[Category: Heme transporter]] | ||
| + | [[Category: Membrane protein]] | ||
Current revision
Helicobacter Hepaticus CcsBA Closed Conformation
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