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2qjy
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2qjy" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qjy, resolution 2.40Å" /> '''Crystal structure of...) |
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caption="2qjy, resolution 2.40Å" /> | caption="2qjy, resolution 2.40Å" /> | ||
'''Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2'''<br /> | '''Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2'''<br /> | ||
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| + | ==Overview== | ||
| + | The cytochrome bc(1) complex (bc(1)) is a major contributor to the proton, motive force across the membrane by coupling electron transfer to proton, translocation. The crystal structures of wild type and mutant bc(1), complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides, (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor, stigmatellin alone or in combination with the quinone reduction (Q(N)), site inhibitor antimycin, were determined. The high quality electron, density permitted assignments of a new metal-binding site to the, cytochrome c(1) subunit and a number of lipid and detergent molecules., Structural differences between Rsbc(1) and its mitochondrial counterparts, are mostly extra membranous and provide a basis for understanding the, function of the predominantly longer sequences in the bacterial subunits., Functional implications for the bc(1) complex are derived from analyses of, 10 independent molecules in various crystal forms and from comparisons, with mitochondrial complexes. | ||
==About this Structure== | ==About this Structure== | ||
| - | 2QJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=BGL:'>BGL</scene>, <scene name='pdbligand=SR:'>SR</scene>, <scene name='pdbligand= | + | 2QJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=BGL:'>BGL</scene>, <scene name='pdbligand=SR:'>SR</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=SMA:'>SMA</scene>, <scene name='pdbligand=LOP:'>LOP</scene>, <scene name='pdbligand=UQ2:'>UQ2</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] Known structural/functional Sites: <scene name='pdbsite=AC1:Bgl+Binding+Site+For+Residue+B+1041'>AC1</scene>, <scene name='pdbsite=AC2:Bgl+Binding+Site+For+Residue+E+1042'>AC2</scene>, <scene name='pdbsite=AC3:Bgl+Binding+Site+For+Residue+G+1043'>AC3</scene>, <scene name='pdbsite=AC4:Bgl+Binding+Site+For+Residue+K+1044'>AC4</scene>, <scene name='pdbsite=AC5:Bgl+Binding+Site+For+Residue+N+1045'>AC5</scene>, <scene name='pdbsite=AC6:Bgl+Binding+Site+For+Residue+P+1046'>AC6</scene>, <scene name='pdbsite=AC7:Sr+Binding+Site+For+Residue+B+1011'>AC7</scene>, <scene name='pdbsite=AC8:Sr+Binding+Site+For+Residue+E+1012'>AC8</scene>, <scene name='pdbsite=AC9:Sr+Binding+Site+For+Residue+H+1013'>AC9</scene>, <scene name='pdbsite=BC1:Sr+Binding+Site+For+Residue+K+1014'>BC1</scene>, <scene name='pdbsite=BC2:Sr+Binding+Site+For+Residue+N+1015'>BC2</scene>, <scene name='pdbsite=BC3:Sr+Binding+Site+For+Residue+Q+1016'>BC3</scene>, <scene name='pdbsite=BC4:Na+Binding+Site+For+Residue+R+2001'>BC4</scene>, <scene name='pdbsite=BC5:Cl+Binding+Site+For+Residue+I+2004'>BC5</scene>, <scene name='pdbsite=BC6:Cl+Binding+Site+For+Residue+R+2005'>BC6</scene>, <scene name='pdbsite=BC7:Hem+Binding+Site+For+Residue+A+501'>BC7</scene>, <scene name='pdbsite=BC8:Hem+Binding+Site+For+Residue+A+502'>BC8</scene>, <scene name='pdbsite=BC9:Hem+Binding+Site+For+Residue+B+301'>BC9</scene>, <scene name='pdbsite=CC1:Fes+Binding+Site+For+Residue+C+200'>CC1</scene>, <scene name='pdbsite=CC2:Hem+Binding+Site+For+Residue+D+501'>CC2</scene>, <scene name='pdbsite=CC3:Hem+Binding+Site+For+Residue+D+502'>CC3</scene>, <scene name='pdbsite=CC4:Hem+Binding+Site+For+Residue+E+301'>CC4</scene>, <scene name='pdbsite=CC5:Fes+Binding+Site+For+Residue+F+200'>CC5</scene>, <scene name='pdbsite=CC6:Hem+Binding+Site+For+Residue+G+501'>CC6</scene>, <scene name='pdbsite=CC7:Hem+Binding+Site+For+Residue+G+502'>CC7</scene>, <scene name='pdbsite=CC8:Hem+Binding+Site+For+Residue+H+301'>CC8</scene>, <scene name='pdbsite=CC9:Fes+Binding+Site+For+Residue+I+200'>CC9</scene>, <scene name='pdbsite=DC1:Hem+Binding+Site+For+Residue+J+501'>DC1</scene>, <scene name='pdbsite=DC2:Hem+Binding+Site+For+Residue+J+502'>DC2</scene>, <scene name='pdbsite=DC3:Hem+Binding+Site+For+Residue+K+301'>DC3</scene>, <scene name='pdbsite=DC4:Fes+Binding+Site+For+Residue+L+200'>DC4</scene>, <scene name='pdbsite=DC5:Hem+Binding+Site+For+Residue+M+501'>DC5</scene>, <scene name='pdbsite=DC6:Hem+Binding+Site+For+Residue+M+502'>DC6</scene>, <scene name='pdbsite=DC7:Hem+Binding+Site+For+Residue+N+301'>DC7</scene>, <scene name='pdbsite=DC8:Fes+Binding+Site+For+Residue+O+200'>DC8</scene>, <scene name='pdbsite=DC9:Hem+Binding+Site+For+Residue+P+501'>DC9</scene>, <scene name='pdbsite=EC1:Hem+Binding+Site+For+Residue+P+502'>EC1</scene>, <scene name='pdbsite=EC2:Hem+Binding+Site+For+Residue+Q+301'>EC2</scene>, <scene name='pdbsite=EC3:Fes+Binding+Site+For+Residue+R+200'>EC3</scene>, <scene name='pdbsite=EC4:Sma+Binding+Site+For+Residue+A+1001'>EC4</scene>, <scene name='pdbsite=EC5:Sma+Binding+Site+For+Residue+D+1002'>EC5</scene>, <scene name='pdbsite=EC6:Sma+Binding+Site+For+Residue+G+1003'>EC6</scene>, <scene name='pdbsite=EC7:Sma+Binding+Site+For+Residue+J+1004'>EC7</scene>, <scene name='pdbsite=EC8:Sma+Binding+Site+For+Residue+M+1005'>EC8</scene>, <scene name='pdbsite=EC9:Sma+Binding+Site+For+Residue+P+1006'>EC9</scene>, <scene name='pdbsite=FC1:Lop+Binding+Site+For+Residue+A+1021'>FC1</scene>, <scene name='pdbsite=FC2:Lop+Binding+Site+For+Residue+D+1022'>FC2</scene>, <scene name='pdbsite=FC3:Lop+Binding+Site+For+Residue+G+1023'>FC3</scene>, <scene name='pdbsite=FC4:Lop+Binding+Site+For+Residue+J+1024'>FC4</scene>, <scene name='pdbsite=FC5:Lop+Binding+Site+For+Residue+M+1025'>FC5</scene>, <scene name='pdbsite=FC6:Lop+Binding+Site+For+Residue+P+1026'>FC6</scene>, <scene name='pdbsite=FC7:Uq2+Binding+Site+For+Residue+A+1101'>FC7</scene>, <scene name='pdbsite=FC8:Uq2+Binding+Site+For+Residue+D+1102'>FC8</scene>, <scene name='pdbsite=FC9:Uq2+Binding+Site+For+Residue+G+1103'>FC9</scene>, <scene name='pdbsite=GC1:Uq2+Binding+Site+For+Residue+J+1104'>GC1</scene>, <scene name='pdbsite=GC2:Uq2+Binding+Site+For+Residue+M+1105'>GC2</scene> and <scene name='pdbsite=GC3:Uq2+Binding+Site+For+Residue+P+1106'>GC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJY OCA]. |
| + | |||
| + | ==Reference== | ||
| + | Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides., Esser L, Elberry M, Zhou F, Yu CA, Yu L, Xia D, J Biol Chem. 2008 Feb 1;283(5):2846-57. Epub 2007 Nov 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18039651 18039651] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:18:31 2008'' |
Revision as of 06:18, 13 February 2008
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Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2
Overview
The cytochrome bc(1) complex (bc(1)) is a major contributor to the proton, motive force across the membrane by coupling electron transfer to proton, translocation. The crystal structures of wild type and mutant bc(1), complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides, (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor, stigmatellin alone or in combination with the quinone reduction (Q(N)), site inhibitor antimycin, were determined. The high quality electron, density permitted assignments of a new metal-binding site to the, cytochrome c(1) subunit and a number of lipid and detergent molecules., Structural differences between Rsbc(1) and its mitochondrial counterparts, are mostly extra membranous and provide a basis for understanding the, function of the predominantly longer sequences in the bacterial subunits., Functional implications for the bc(1) complex are derived from analyses of, 10 independent molecules in various crystal forms and from comparisons, with mitochondrial complexes.
About this Structure
2QJY is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , , , and as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Known structural/functional Sites: , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides., Esser L, Elberry M, Zhou F, Yu CA, Yu L, Xia D, J Biol Chem. 2008 Feb 1;283(5):2846-57. Epub 2007 Nov 26. PMID:18039651
Page seeded by OCA on Wed Feb 13 08:18:31 2008
Categories: Protein complex | Rhodobacter sphaeroides | Ubiquinol--cytochrome-c reductase | Esser, L. | Xia, D. | BGL | CL | FES | HEM | LOP | NA | SMA | SR | UQ2 | 1 c-term tm helix rieske | 1 n-term tm helix | 8 tm helixces cytochrome c1 | Cytochrome b | Oxidoreductase
