2bs3

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[[Image:2bs3.gif|left|200px]]<br /><applet load="2bs3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bs3.gif|left|200px]]
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caption="2bs3, resolution 2.19&Aring;" />
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'''GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''<br />
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{{Structure
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|PDB= 2bs3 |SIZE=350|CAPTION= <scene name='initialview01'>2bs3</scene>, resolution 2.19&Aring;
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|SITE= <scene name='pdbsite=AC1:Lmt+Binding+Site+For+Chain+F'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''GLU C180-> GLN VARIANT QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=CIT:'>CIT</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=F3S:'>F3S</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=LMT:'>LMT</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Lmt+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS3 OCA].
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2BS3 is a [[Protein complex]] structure of sequences 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==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/16380425 16380425]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Succinate dehydrogenase]]
[[Category: Succinate dehydrogenase]]
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[[Category: NA]]
[[Category: NA]]
[[Category: SF4]]
[[Category: SF4]]
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[[Category: 2fe-2s]]
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[[Category: 2fe-2]]
[[Category: 3d-structure]]
[[Category: 3d-structure]]
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[[Category: 3fe-4s]]
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[[Category: 3fe-4]]
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[[Category: 4fe-4s]]
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[[Category: 4fe-4]]
[[Category: citric acid cycle]]
[[Category: citric acid cycle]]
[[Category: dihaem cytochrome b]]
[[Category: dihaem cytochrome b]]
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[[Category: tricarboxylic acid cycle]]
[[Category: tricarboxylic acid cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:03 2008''

Revision as of 14:06, 20 March 2008

Image:2bs3.gif


PDB ID 2bs3

Drag the structure with the mouse to rotate
, resolution 2.19Å
Sites:
Ligands: , , , , , , and
Activity: Succinate dehydrogenase, with EC number 1.3.99.1
Coordinates: save as pdb, mmCIF, xml



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

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