2bs3

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[[Image:2bs3.gif|left|200px]]
[[Image:2bs3.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2bs3 |SIZE=350|CAPTION= <scene name='initialview01'>2bs3</scene>, resolution 2.19&Aring;
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The line below this paragraph, containing "STRUCTURE_2bs3", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Lmt+Binding+Site+For+Chain+F'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2bs3| PDB=2bs3 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs3 OCA], [http://www.ebi.ac.uk/pdbsum/2bs3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bs3 RCSB]</span>
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}}
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'''GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''
'''GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''
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[[Category: 3fe-4]]
[[Category: 3fe-4]]
[[Category: 4fe-4]]
[[Category: 4fe-4]]
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[[Category: citric acid cycle]]
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[[Category: Citric acid cycle]]
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[[Category: dihaem cytochrome b]]
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[[Category: Dihaem cytochrome b]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: fad]]
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[[Category: Fad]]
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[[Category: flavoprotein]]
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[[Category: Flavoprotein]]
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[[Category: fumarate reductase]]
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[[Category: Fumarate reductase]]
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[[Category: heme]]
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[[Category: Heme]]
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[[Category: ion-sulphur protein]]
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[[Category: Ion-sulphur protein]]
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[[Category: iron]]
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[[Category: Iron]]
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[[Category: iron-sulfur]]
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[[Category: Iron-sulfur]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: respiratory chain]]
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[[Category: Respiratory chain]]
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[[Category: succinate dehydrogenase]]
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[[Category: Succinate dehydrogenase]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: tricarboxylic acid cycle]]
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[[Category: Tricarboxylic acid cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:43:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:10:55 2008''
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Revision as of 17:43, 3 May 2008

Image:2bs3.gif

Template:STRUCTURE 2bs3

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 purified enzymes display approximately 1/10 of the specific quinol oxidation activity of the wild-type enzyme and unchanged quinol Michaelis constants, K(m). The refined x-ray crystal structures at 2.19 A and 2.76 A resolution, respectively, rule out major structural changes to account for these experimental observations. Changes in the oxidation-reduction heme midpoint potential allow the conclusion that deprotonation of Glu-C180 in the wild-type enzyme facilitates the reoxidation of the reduced high-potential heme. Comparison of solvent isotope effects indicates that a rate-limiting proton transfer step in the wild-type enzyme is lost in the Glu-C180 --> Gln variant. The results provide experimental evidence for the validity of the E pathway hypothesis and for a crucial functional role of Glu-C180.

About this Structure

2BS3 is a Protein complex structure of sequences from Wolinella succinogenes. 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 Sat May 3 20:43:19 2008

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