1zrt: Difference between revisions
New page: left|200px<br /><applet load="1zrt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zrt, resolution 3.50Å" /> '''Rhodobacter capsulat... |
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[[Image:1zrt.gif|left|200px]]<br /><applet load="1zrt" size=" | [[Image:1zrt.gif|left|200px]]<br /><applet load="1zrt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1zrt, resolution 3.50Å" /> | caption="1zrt, resolution 3.50Å" /> | ||
'''Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound'''<br /> | '''Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound'''<br /> | ||
==Overview== | ==Overview== | ||
Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a | Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a widespread, membrane integral enzyme that plays a crucial role during photosynthesis and respiration. It is one of the major contributors of the electrochemical proton gradient, which is subsequently used for ATP synthesis. The simplest form of the cyt bc (1) is found in bacteria, and it contains only the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its homologues from mitochondria and chloroplast. Using the bacterial enzyme structure, we highlight the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes. In addition, we discuss the locations of currently known critical mutations, and their implications in terms of the cyt bc (1) catalysis. | ||
==About this Structure== | ==About this Structure== | ||
1ZRT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with HEM, SMA, HEC and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Full crystallographic information is available from [http:// | 1ZRT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=SMA:'>SMA</scene>, <scene name='pdbligand=HEC:'>HEC</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Ubiquinol--cytochrome-c reductase]] | [[Category: Ubiquinol--cytochrome-c reductase]] | ||
[[Category: Berry, E | [[Category: Berry, E A.]] | ||
[[Category: Daldal, F.]] | [[Category: Daldal, F.]] | ||
[[Category: Huang, L | [[Category: Huang, L S.]] | ||
[[Category: Pon, N | [[Category: Pon, N G.]] | ||
[[Category: Saechao, L | [[Category: Saechao, L K.]] | ||
[[Category: Valkova-Valchanov, M.]] | [[Category: Valkova-Valchanov, M.]] | ||
[[Category: FES]] | [[Category: FES]] | ||
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[[Category: stigmatellin]] | [[Category: stigmatellin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:18:27 2008'' |
Revision as of 17:18, 21 February 2008
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Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound
OverviewOverview
Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a widespread, membrane integral enzyme that plays a crucial role during photosynthesis and respiration. It is one of the major contributors of the electrochemical proton gradient, which is subsequently used for ATP synthesis. The simplest form of the cyt bc (1) is found in bacteria, and it contains only the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its homologues from mitochondria and chloroplast. Using the bacterial enzyme structure, we highlight the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes. In addition, we discuss the locations of currently known critical mutations, and their implications in terms of the cyt bc (1) catalysis.
About this StructureAbout this Structure
1ZRT is a Protein complex structure of sequences from Rhodobacter capsulatus with , , and as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Full crystallographic information is available from OCA.
ReferenceReference
X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts., Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, Daldal F, Photosynth Res. 2004;81(3):251-75. PMID:16034531
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OCA- Pages with broken file links
- Protein complex
- Rhodobacter capsulatus
- Ubiquinol--cytochrome-c reductase
- Berry, E A.
- Daldal, F.
- Huang, L S.
- Pon, N G.
- Saechao, L K.
- Valkova-Valchanov, M.
- FES
- HEC
- HEM
- SMA
- Complex iii
- Cytochrome b
- Cytochrome bc1
- Cytochrome c1
- Heme protein
- Membrane protein
- Oxidoreductase
- Redox enzyme
- Respiratory chain
- Rieske iron sulfur protein
- Stigmatellin