7ose
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ==== | + | ==cytochrome bd-II type oxidase with bound aurachin D== |
| - | <StructureSection load='7ose' size='340' side='right'caption='[[7ose]]' scene=''> | + | <StructureSection load='7ose' size='340' side='right'caption='[[7ose]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ose]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW25113 Escherichia coli BW25113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OSE FirstGlance]. <br> |
| - | </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=7ose FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ose OCA], [https://pdbe.org/7ose PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ose RCSB], [https://www.ebi.ac.uk/pdbsum/7ose PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ose ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0NI:Aurachin+D'>0NI</scene>, <scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene>, <scene name='pdbligand=HEB:HEME+B/C'>HEB</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</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=7ose FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ose OCA], [https://pdbe.org/7ose PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ose RCSB], [https://www.ebi.ac.uk/pdbsum/7ose PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ose ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/APPC_ECOLI APPC_ECOLI] A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.<ref>PMID:19542282</ref> <ref>PMID:21987791</ref> <ref>PMID:22843529</ref> <ref>PMID:8626304</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytochrome bd quinol:O(2) oxidoreductases are respiratory terminal oxidases so far only identified in prokaryotes, including several pathogenic bacteria. Escherichia coli contains two bd oxidases of which only the bd-I type is structurally characterized. Here, we report the structure of the Escherichia coli cytochrome bd-II type oxidase with the bound inhibitor aurachin D as obtained by electron cryo-microscopy at 3 A resolution. The oxidase consists of subunits AppB, C and X that show an architecture similar to that of bd-I. The three heme cofactors are found in AppC, while AppB is stabilized by a structural ubiquinone-8 at the homologous positions. A fourth subunit present in bd-I is lacking in bd-II. Accordingly, heme b(595) is exposed to the membrane but heme d embedded within the protein and showing an unexpectedly high redox potential is the catalytically active centre. The structure of the Q-loop is fully resolved, revealing the specific aurachin binding. | ||
| + | |||
| + | Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D.,Grauel A, Kagi J, Rasmussen T, Makarchuk I, Oppermann S, Moumbock AFA, Wohlwend D, Muller R, Melin F, Gunther S, Hellwig P, Bottcher B, Friedrich T Nat Commun. 2021 Nov 11;12(1):6498. doi: 10.1038/s41467-021-26835-2. PMID:34764272<ref>PMID:34764272</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ose" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli BW25113]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Boettcher B]] |
| + | [[Category: Friedrich T]] | ||
| + | [[Category: Grauel A]] | ||
| + | [[Category: Kaegi J]] | ||
| + | [[Category: Rasmussen T]] | ||
| + | [[Category: Wohlwend D]] | ||
Current revision
cytochrome bd-II type oxidase with bound aurachin D
| |||||||||||
