25vk: Difference between revisions
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==Bacteroides thetaiotaomicron CcsBA mutant W703C== | |||
<StructureSection load='25vk' size='340' side='right'caption='[[25vk]], [[Resolution|resolution]] 2.91Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[25vk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=25VK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=25VK 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]] 2.91Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=25vk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=25vk OCA], [https://pdbe.org/25vk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=25vk RCSB], [https://www.ebi.ac.uk/pdbsum/25vk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=25vk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q89ZE7_BACTN Q89ZE7_BACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome c biogenesis in bacteria relies on complex membrane-bound machineries that facilitate the covalent attachment of heme to apocytochrome c. System II, mediated by the bifunctional protein CcsBA, is prevalent in Gram-positive and some Gram-negative bacteria, as well as chloroplasts. Here, we report a 2.9 A resolution cryo-EM structure of a W703C mutant of CcsBA from Bacteroides thetaiotaomicron, revealing its conformation in the heme-loaded, closed state. Comparative analysis with the previously published Helicobacter hepaticus CcsBA structure shows a conserved membrane architecture and WxWD domain organization, but notable differences in the arrangement of the periplasmic domain and the active site configuration. The W703C mutation allowed heme occupancy in the active site without inducing the open conformation, implicating the native W703 in regulating structural transitions critical for heme attachment. Our findings suggest that while the open conformation facilitates heme ligation, it is not essential for heme translocation. This work expands the understanding of structure-function relationships in System II cytochrome c maturation and highlights the potential regulatory role of the periplasmic domain conformational dynamics. | |||
Heme handling in the system II heme lyase CcsBA from Bacteroides thetaiotaomicron.,Seifermann J, Ilcu L, Moog C, Zhang L, Einsle O J Biol Inorg Chem. 2026 Aug 25. doi: 10.1007/s00775-026-02171-y. PMID:42640290<ref>PMID:42640290</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 25vk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides thetaiotaomicron VPI-5482]] | |||
[[Category: Large Structures]] | |||
[[Category: Einsle O]] | |||
[[Category: Ilcu L]] | |||
[[Category: Moog C]] | |||
[[Category: Seifermann J]] | |||
[[Category: Zhang L]] | |||
