2bs3
From Proteopedia
(New page: 200px<br /> <applet load="2bs3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bs3, resolution 2.19Å" /> '''GLU C180-> GLN VARI...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BS3 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]] with NA, FAD, CIT, FES, F3S, SF4, HEM and LMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA]]. | + | 2BS3 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]] with NA, FAD, CIT, FES, F3S, SF4, HEM and LMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA]]. |
==Reference== | ==Reference== | ||
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase., Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16380425 16380425] | Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase., Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16380425 16380425] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Succinate dehydrogenase]] | ||
[[Category: Wolinella succinogenes]] | [[Category: Wolinella succinogenes]] | ||
[[Category: Lancaster, C.R.D.]] | [[Category: Lancaster, C.R.D.]] | ||
| Line 44: | Line 45: | ||
[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:40:53 2007'' |
Revision as of 10:36, 30 October 2007
|
GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES
Overview
Reconciliation of apparently contradictory experimental results obtained, on the quinol:fumarate reductase, a diheme-containing respiratory membrane, protein complex from Wolinella succinogenes, was previously obtained by, the proposal of the so-called "E pathway hypothesis." According to this, hypothesis, transmembrane electron transfer via the heme groups is, strictly coupled to cotransfer of protons via a transiently established, pathway thought to contain the side chain of residue Glu-C180 as the most, prominent component. Here we demonstrate that, after replacement of, Glu-C180 with Gln or Ile by site-directed mutagenesis, the resulting, mutants are unable to grow on fumarate, and the membrane-bound variant, enzymes lack quinol oxidation activity. Upon solubilization, however, the, ... [(full description)]
About this Structure
2BS3 is a [Protein complex] structure of sequences from [Wolinella succinogenes] with NA, FAD, CIT, FES, F3S, SF4, HEM and LMT as [ligands]. Active as [Succinate dehydrogenase], with EC number [1.3.99.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase., Lancaster CR, Sauer US, Gross R, Haas AH, Graf J, Schwalbe H, Mantele W, Simon J, Madej MG, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18860-5. PMID:16380425
Page seeded by OCA on Tue Oct 30 12:40:53 2007
Categories: Protein complex | Succinate dehydrogenase | Wolinella succinogenes | Lancaster, C.R.D. | CIT | F3S | FAD | FES | HEM | LMT | NA | SF4 | 2fe-2s | 3d-structure | 3fe-4s | 4fe-4s | 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
