1cyx

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Revision as of 10:41, 14 July 2021

QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II WITH ENGINEERED CU-A BINDING SITE)(CYOA)

Structural highlights

1cyx is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CYOA_ECOLI] Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cytochrome oxidase is a membrane protein complex that catalyzes reduction of molecular oxygen to water and utilizes the free energy of this reaction to generate a transmembrane proton gradient during respiration. The electron entry site in subunit II is a mixed-valence dinuclear copper center in enzymes that oxidize cytochrome c. This center has been lost during the evolution of the quinoloxidizing branch of cytochrome oxidases but can be restored by engineering. Herein we describe the crystal structures of the periplasmic fragment from the wild-type subunit II (CyoA) of Escherichia coli quinol oxidase at 2.5-A resolution and of the mutant with the engineered dinuclear copper center (purple CyoA) at 2.3-A resolution. CyoA is folded as an 11-stranded mostly antiparallel beta-sandwich followed by three alpha-helices. The dinuclear copper center is located at the loops between strands beta 5-beta 6 and beta 9-beta 10. The two coppers are at a 2.5-A distance and symmetrically coordinated to the main ligands that are two bridging cysteines and two terminal histidines. The residues that are distinct in cytochrome c and quinol oxidases are around the dinuclear copper center. Structural comparison suggests a common ancestry for subunit II of cytochrome oxidase and blue copper-binding proteins.

Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center.,Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):11955-9. PMID:8618822^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Matsushita K, Patel L, Gennis RB, Kaback HR. Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli. Proc Natl Acad Sci U S A. 1983 Aug;80(16):4889-93. PMID:6308657
↑ Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:http://dx.doi.org/10.1128/JB.00562-09
↑ Sharma P, Hellingwerf KJ, de Mattos MJ, Bekker M. Uncoupling of substrate-level phosphorylation in Escherichia coli during glucose-limited growth. Appl Environ Microbiol. 2012 Oct;78(19):6908-13. doi: 10.1128/AEM.01507-12. Epub , 2012 Jul 27. PMID:22843529 doi:http://dx.doi.org/10.1128/AEM.01507-12
↑ Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):11955-9. PMID:8618822

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cyx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cyx' size='340' side='right'caption='[[1cyx]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CYX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cyx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CYX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene></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=1cyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyx OCA], [http://pdbe.org/1cyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cyx RCSB], [http://www.ebi.ac.uk/pdbsum/1cyx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cyx ProSAT]</span></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=1cyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyx OCA], [https://pdbe.org/1cyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cyx RCSB], [https://www.ebi.ac.uk/pdbsum/1cyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cyx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYOA_ECOLI CYOA_ECOLI]] Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.<ref>PMID:6308657</ref> <ref>PMID:19542282</ref> <ref>PMID:22843529</ref>
+[[https://www.uniprot.org/uniprot/CYOA_ECOLI CYOA_ECOLI]] Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron.<ref>PMID:6308657</ref> <ref>PMID:19542282</ref> <ref>PMID:22843529</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1cyx

From Proteopedia

Revision as of 10:41, 14 July 2021

QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II WITH ENGINEERED CU-A BINDING SITE)(CYOA)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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