1cyw: Difference between revisions

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[[Image:1cyw.png|left|200px]]


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==QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II) (CYOA)==
The line below this paragraph, containing "STRUCTURE_1cyw", creates the "Structure Box" on the page.
<StructureSection load='1cyw' size='340' side='right'caption='[[1cyw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1cyw]] is a 1 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=1CYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CYW FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyw OCA], [https://pdbe.org/1cyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cyw RCSB], [https://www.ebi.ac.uk/pdbsum/1cyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cyw ProSAT]</span></td></tr>
{{STRUCTURE_1cyw|  PDB=1cyw  |  SCENE=  }}
</table>
 
== Function ==
===QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II) (CYOA)===
[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]]
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Check<jmol>
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{{ABSTRACT_PUBMED_8618822}}
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  </jmolCheckbox>
==About this Structure==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cyw ConSurf].
1CYW is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYW OCA].  
<div style="clear:both"></div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:8618822</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Kelly, M.]]
[[Category: Large Structures]]
[[Category: Lappalainen, P.]]
[[Category: Kelly M]]
[[Category: Saraste, M.]]
[[Category: Lappalainen P]]
[[Category: Sauer-Eriksson, E.]]
[[Category: Saraste M]]
[[Category: Wilmanns, M.]]
[[Category: Sauer-Eriksson E]]
[[Category: Electron transport]]
[[Category: Wilmanns M]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:37:25 2009''

Latest revision as of 09:46, 7 February 2024

QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II) (CYOA)QUINOL OXIDASE (PERIPLASMIC FRAGMENT OF SUBUNIT II) (CYOA)

Structural highlights

1cyw is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
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.

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

1cyw, resolution 2.50Å

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