2fyn
From Proteopedia
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|PDB= 2fyn |SIZE=350|CAPTION= <scene name='initialview01'>2fyn</scene>, resolution 3.20Å | |PDB= 2fyn |SIZE=350|CAPTION= <scene name='initialview01'>2fyn</scene>, resolution 3.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LOP:(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>LOP</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= petB, fbcB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), petC, fbcC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | |GENE= petB, fbcB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), petC, fbcC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]), petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qcr|1qcr]], [[1l0n|1l0n]], [[1sqx|1sqx]], [[1zrt|1zrt]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyn OCA], [http://www.ebi.ac.uk/pdbsum/2fyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fyn RCSB]</span> | ||
}} | }} | ||
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[[Category: Esser, L.]] | [[Category: Esser, L.]] | ||
[[Category: Xia, D.]] | [[Category: Xia, D.]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: LOP]] | ||
| - | [[Category: SMA]] | ||
[[Category: functional dimer]] | [[Category: functional dimer]] | ||
[[Category: transmembrane helice]] | [[Category: transmembrane helice]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:09:26 2008'' |
Revision as of 00:09, 31 March 2008
| |||||||
| , resolution 3.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | petB, fbcB (Rhodobacter sphaeroides), petC, fbcC (Rhodobacter sphaeroides), petA, fbcF (Rhodobacter sphaeroides) | ||||||
| Activity: | Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 | ||||||
| Related: | 1qcr, 1l0n, 1sqx, 1zrt
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of the double mutant Rhodobacter Sphaeroides bc1 complex
Overview
In the cytochrome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites constitutes a key component of the mechanism that achieves the separation of the two electrons in a substrate molecule at the quinol oxidation (Q(o)) site. The question remaining is how the motion of ISP is controlled so that only one electron enters the thermodynamically favorable chain via ISP. An analysis of eight structures of mitochondrial bc(1) with bound Q(o) site inhibitors revealed that the presence of inhibitors causes a bidirectional repositioning of the cd1 helix in the cytochrome b subunit. As the cd1 helix forms a major part of the ISP binding crater, any positional shift of this helix modulates the ability of cytochrome b to bind ISP. The analysis also suggests a mechanism for reversal of the ISP fixation when the shape complementarity is significantly reduced after a positional reorientation of the reaction product quinone. The importance of shape complementarity in this mechanism was confirmed by functional studies of bc(1) mutants and by a structure determination of the bacterial form of bc(1). A mechanism for the high fidelity of the bifurcated electron transfer is proposed.
About this Structure
2FYN is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
Reference
Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex., Esser L, Gong X, Yang S, Yu L, Yu CA, Xia D, Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13045-50. Epub 2006 Aug 21. PMID:16924113
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