View source for 5djq


==The structure of CBB3 cytochrome oxidase.==
<StructureSection load='5djq' size='340' side='right'caption='[[5djq]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5djq]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] and [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri_ATCC_14405_=_CCUG_16156 Pseudomonas stutzeri ATCC 14405 = CCUG 16156]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5djq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djq OCA], [https://pdbe.org/5djq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5djq RCSB], [https://www.ebi.ac.uk/pdbsum/5djq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5djq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCON1_STUST CCON1_STUST] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations.

The structure of cbb3 cytochrome oxidase provides insights into proton pumping.,Buschmann S, Warkentin E, Xie H, Langer JD, Ermler U, Michel H Science. 2010 Jul 16;329(5989):327-30. Epub 2010 Jun 24. PMID:20576851<ref>PMID:20576851</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5djq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]]
[[Category: Buschmann S]]
[[Category: Ermler U]]
[[Category: Kohlstaedt M]]
[[Category: Langer JD]]
[[Category: Michel H]]
[[Category: Warkentin E]]
[[Category: Xie H]]