View source for 6pw0


==Cytochrome C oxidase delta 6 mutant==
<StructureSection load='6pw0' size='340' side='right'caption='[[6pw0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pw0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhos4 Rhos4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PW0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=HTH:(2S,3R)-HEPTANE-1,2,3-TRIOL'>HTH</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=TRD:TRIDECANE'>TRD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gsm|2gsm]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coxI, RSP_1877 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4]), coxII, RSP_1826 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272943 RHOS4])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pw0 OCA], [http://pdbe.org/6pw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pw0 RCSB], [http://www.ebi.ac.uk/pdbsum/6pw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pw0 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q3J5G0_RHOS4 Q3J5G0_RHOS4]] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).[RuleBase:RU004024] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Data from earlier studies showed that minor structural changes at the surface of cytochrome c oxidase, near one of the proton-input pathways (the D pathway), result in dramatically decreased activity and a lower proton-pumping stoichiometry. To further investigate how changes around the D pathway orifice influence functionality of the enzyme, here we modified the nearby C-terminal loop of subunit I of the Rhodobacter sphaeroides cytochrome c oxidase. Removal of 16 residues form this flexible surface loop resulted in a decrease in the proton-pumping stoichiometry to &lt;50% of that of the wild-type enzyme. Replacement of the protonatable residue Glu552, part of the same loop, by an Ala, resulted in a similar decrease in the proton-pumping stoichiometry without loss of the O2-reduction activity or changes in the proton-uptake kinetics. The data show that minor structural changes at the orifice of the D pathway, at a distance of ~40A from the proton gate of cytochrome c oxidase, may alter the proton-pumping stoichiometry of the enzyme.

Structural changes at the surface of cytochrome c oxidase alter the proton-pumping stoichiometry.,Berg J, Liu J, Svahn E, Ferguson-Miller S, Brzezinski P Biochim Biophys Acta Bioenerg. 2019 Nov 13:148116. doi:, 10.1016/j.bbabio.2019.148116. PMID:31733183<ref>PMID:31733183</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pw0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cytochrome-c oxidase]]
[[Category: Large Structures]]
[[Category: Rhos4]]
[[Category: Ferguson-Miller, S]]
[[Category: Liu, J]]
[[Category: Electron transfer]]
[[Category: Membrane protein]]
[[Category: Oxidase]]
[[Category: Oxidoreductase]]
[[Category: Proton pumping]]