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| - | [[Image:1ntk.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ntk| PDB=1ntk | SCENE= }} | | {{STRUCTURE_1ntk| PDB=1ntk | SCENE= }} |
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| - | '''Crystal Structure of Mitochondrial Cytochrome bc1 in Complex with Antimycin A1'''
| + | ===Crystal Structure of Mitochondrial Cytochrome bc1 in Complex with Antimycin A1=== |
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| - | ==Overview==
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| - | Cytochrome bc(1) is an integral membrane protein complex essential to cellular respiration and photosynthesis. The Q cycle reaction mechanism of bc(1) postulates a separated quinone reduction (Q(i)) and quinol oxidation (Q(o)) site. In a complete catalytic cycle, a quinone molecule at the Q(i) site receives two electrons from the b(H) heme and two protons from the negative side of the membrane; this process is specifically inhibited by antimycin A and NQNO. The structures of bovine mitochondrial bc(1) in the presence or absence of bound substrate ubiquinone and with either the bound antimycin A(1) or NQNO were determined and refined. A ubiquinone with its first two isoprenoid repeats and an antimycin A(1) were identified in the Q(i) pocket of the substrate and inhibitor bound structures, respectively; the NQNO, on the other hand, was identified in both Q(i) and Q(o) pockets in the inhibitor complex. The two inhibitors occupied different portions of the Q(i) pocket and competed with substrate for binding. In the Q(o) pocket, the NQNO behaves similarly to stigmatellin, inducing an iron-sulfur protein conformational arrest. Extensive binding interactions and conformational adjustments of residues lining the Q(i) pocket provide a structural basis for the high affinity binding of antimycin A and for phenotypes of inhibitor resistance. A two-water-mediated ubiquinone protonation mechanism is proposed involving three Q(i) site residues His(201), Lys(227), and Asp(228).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12885240}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12885240 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12885240}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Yu, L.]] | | [[Category: Yu, L.]] |
| | [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:57:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:45:16 2008'' |
Revision as of 00:45, 29 July 2008
Template:STRUCTURE 1ntk
Crystal Structure of Mitochondrial Cytochrome bc1 in Complex with Antimycin A1
Template:ABSTRACT PUBMED 12885240
About this Structure
1NTK is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis for the quinone reduction in the bc1 complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc1 with bound substrate and inhibitors at the Qi site., Gao X, Wen X, Esser L, Quinn B, Yu L, Yu CA, Xia D, Biochemistry. 2003 Aug 5;42(30):9067-80. PMID:12885240
Page seeded by OCA on Tue Jul 29 03:45:16 2008
