View source for 9hwk


==Structure of the Cytochrome o ubiquinol oxidase embedded in the nanodisc==
<StructureSection load='9hwk' size='340' side='right'caption='[[9hwk]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hwk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HWK 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]] 2.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HEO:HEME+O'>HEO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9hwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hwk OCA], [https://pdbe.org/9hwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hwk RCSB], [https://www.ebi.ac.uk/pdbsum/9hwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hwk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYOB_ECO57 CYOB_ECO57] Cytochrome bo(3) ubiquinol oxidase is the terminal enzyme in the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Catalyzes the four-electron reduction of O2 to water, using a ubiquinol as a membrane soluble electron donor for molecular oxygen reduction; ubiquinol-8 is the natural substrate for E.coli. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron and generating a proton motive force. All the redox centers of this enzyme complex are located within the largest subunit, subunit I. Protons are probably pumped via D- and K- channels found in this subunit.[UniProtKB:P0ABI8]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Mim C]]
[[Category: Murthy AV]]
[[Category: Zhang Q]]