2bs3: Difference between revisions
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[[Image:2bs3.png|left|200px]] | [[Image:2bs3.png|left|200px]] | ||
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{{STRUCTURE_2bs3| PDB=2bs3 | SCENE= }} | {{STRUCTURE_2bs3| PDB=2bs3 | SCENE= }} | ||
===GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES=== | ===GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES=== | ||
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==About this Structure== | ==About this Structure== | ||
[[2bs3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:16380425</ref><references group="xtra"/> | <ref group="xtra">PMID:16380425</ref><ref group="xtra">PMID:14630313</ref><ref group="xtra">PMID:12409197</ref><ref group="xtra">PMID:11248702</ref><ref group="xtra">PMID:11186225</ref><ref group="xtra">PMID:10586875</ref><references group="xtra"/> | ||
[[Category: Succinate dehydrogenase]] | [[Category: Succinate dehydrogenase]] | ||
[[Category: Wolinella succinogenes]] | [[Category: Wolinella succinogenes]] | ||
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[[Category: Ion-sulphur protein]] | [[Category: Ion-sulphur protein]] | ||
[[Category: Iron]] | [[Category: Iron]] | ||
[[Category: Iron-sulfur]] | [[Category: Iron- sulfur]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
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[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Tricarboxylic acid cycle]] | [[Category: Tricarboxylic acid cycle]] | ||
Revision as of 18:13, 14 March 2011
GLU C180 -> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Template:ABSTRACT PUBMED 16380425
About this Structure
2bs3 is a 6 chain structure with sequence from Wolinella succinogenes. Full crystallographic information is available from OCA.
Reference
- Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG. Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:16380425 doi:10.1073/pnas.0509711102
- Lancaster CR. Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase. FEBS Lett. 2003 Nov 27;555(1):21-8. PMID:14630313
- Lancaster CR. Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer. Biochim Biophys Acta. 2002 Oct 11;1565(2):215-31. PMID:12409197
- Lancaster CR, Gross R, Simon J. A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702
- Lancaster CR, Gorss R, Haas A, Ritter M, Mantele W, Simon J, Kroger A. Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase. Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13051-6. PMID:11186225
- Lancaster CR, Kroger A, Auer M, Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature. 1999 Nov 25;402(6760):377-85. PMID:10586875 doi:10.1038/46483
Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Pages with broken file links
- Succinate dehydrogenase
- Wolinella succinogenes
- Lancaster, C R.D.
- 2fe-2
- 3d-structure
- 3fe-4
- 4fe-4
- Citric acid cycle
- Dihaem cytochrome b
- Electron transport
- Fad
- Flavoprotein
- Fumarate reductase
- Heme
- Ion-sulphur protein
- Iron
- Iron- sulfur
- Metal-binding
- Oxidoreductase
- Respiratory chain
- Transmembrane
- Tricarboxylic acid cycle
