We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1sqp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sqp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sqp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sqp| PDB=1sqp | SCENE= }}
{{STRUCTURE_1sqp| PDB=1sqp | SCENE= }}
-
'''Crystal Structure Analysis of Bovine Bc1 with Myxothiazol'''
+
===Crystal Structure Analysis of Bovine Bc1 with Myxothiazol===
-
==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==
==About this Structure==
Line 35: Line 39:
[[Category: Membrane protein]]
[[Category: Membrane protein]]
[[Category: Qo inhibitor]]
[[Category: Qo inhibitor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:01:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:45:22 2008''

Revision as of 03:45, 28 July 2008

Image:1sqp.png

Template:STRUCTURE 1sqp

Crystal Structure Analysis of Bovine Bc1 with Myxothiazol

Template:ABSTRACT PUBMED 15312779

About this Structure

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

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:15312779

Page seeded by OCA on Mon Jul 28 06:45:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sqp"
Personal tools