1sqv: Difference between revisions

Revision as of 12:39, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sqv.png

Template:STRUCTURE 1sqv

Crystal Structure Analysis of Bovine Bc1 with UHDBTCrystal Structure Analysis of Bovine Bc1 with UHDBT

Template:ABSTRACT PUBMED 15312779

About this StructureAbout this Structure

1SQV is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex., Esser L, Quinn B, Li YF, Zhang M, Elberry M, Yu L, Yu CA, Xia D, J Mol Biol. 2004 Jul 30;341(1):281-302. PMID:15312779

Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria., Xia D, Yu CA, Kim H, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J, Science. 1997 Jul 4;277(5322):60-6. PMID:9204897

The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition., Gao X, Wen X, Yu C, Esser L, Tsao S, Quinn B, Zhang L, Yu L, Xia D, Biochemistry. 2002 Oct 1;41(39):11692-702. PMID:12269811

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OCA

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-[[Image:1sqv.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1sqv|  PDB=1sqv  |  SCENE=  }}
-'''Crystal Structure Analysis of Bovine Bc1 with UHDBT'''
+===Crystal Structure Analysis of Bovine Bc1 with UHDBT===
-==Overview==
+<!--
-Cytochrome bc(1) is an integral membrane protein complex essential for cellular respiration and photosynthesis; it couples electron transfer from quinol to cytochrome c to proton translocation across the membrane. Specific bc(1) inhibitors have not only played crucial roles in elucidating the mechanism of bc(1) function but have also provided leads for the development of novel antibiotics. Crystal structures of bovine bc(1) in complex with the specific Q(o) site inhibitors azoxystrobin, MOAS, myxothiazol, stigmatellin and 5-undecyl-6-hydroxy-4,7-dioxobenzothiazole were determined. Interactions, conformational changes and possible mechanisms of resistance, specific to each inhibitor, were defined. Residues and secondary structure elements that are capable of discriminating different classes of Q(o) site inhibitors were identified for the cytochrome b subunit. Directions in the displacement of the cd1 helix of cytochrome b subunit in response to various Q(o) site inhibitors were correlated to the binary conformational switch of the extrinsic domain of the iron-sulfur protein subunit. The new structural information, together with structures previously determined, provide a basis that, combined with biophysical and mutational data, suggest a modification to the existing classification of bc(1) inhibitors. bc(1) inhibitors are grouped into three classes: class P inhibitors bind to the Q(o) site, class N inhibitors bind to the Q(i) site and the class PN inhibitors target both sites. Class P contains two subgroups, Pm and Pf, that are distinct by their ability to induce mobile or fixed conformation of iron-sulfur protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_15312779}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15312779 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15312779}}
 ==About this Structure==
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 ==Reference==
 Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex., Esser L, Quinn B, Li YF, Zhang M, Elberry M, Yu L, Yu CA, Xia D, J Mol Biol. 2004 Jul 30;341(1):281-302. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15312779 15312779]
+Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria., Xia D, Yu CA, Kim H, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J, Science. 1997 Jul 4;277(5322):60-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9204897 9204897]
+The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition., Gao X, Wen X, Yu C, Esser L, Tsao S, Quinn B, Zhang L, Yu L, Xia D, Biochemistry. 2002 Oct 1;41(39):11692-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12269811 12269811]
 [[Category: Bos taurus]]
 [[Category: Protein complex]]
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 [[Category: Membrane protein]]
 [[Category: Qo inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:02:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:39:03 2008''