4bgt

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m (Protected "4bgt" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4bgt| PDB=4bgt | SCENE= }}
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===1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus===
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{{ABSTRACT_PUBMED_22319152}}
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The entry 4bgt is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/MDH_CHLAA MDH_CHLAA]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
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Authors: Talon, R., Madern, D., Girard, E.
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==About this Structure==
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[[4bgt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chloroflexus_aurantiacus Chloroflexus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BGT OCA].
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Description: 1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus
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==Reference==
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<ref group="xtra">PMID:022319152</ref><ref group="xtra">PMID:020888835</ref><ref group="xtra">PMID:017211074</ref><ref group="xtra">PMID:012581646</ref><references group="xtra"/><references/>
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[[Category: Chloroflexus aurantiacus]]
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[[Category: Malate dehydrogenase]]
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[[Category: Girard, E.]]
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[[Category: Madern, D.]]
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[[Category: Talon, R.]]
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[[Category: Oxidoreductase]]
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[[Category: Thermophile]]
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[[Category: Tricarboxylic acid cycle]]

Revision as of 11:26, 24 April 2013

Template:STRUCTURE 4bgt

Contents

1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus

Template:ABSTRACT PUBMED 22319152

Function

[MDH_CHLAA] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]

About this Structure

4bgt is a 2 chain structure with sequence from Chloroflexus aurantiacus. Full crystallographic information is available from OCA.

Reference

  • Colletier JP, Aleksandrov A, Coquelle N, Mraihi S, Mendoza-Barbera E, Field M, Madern D. Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions. Mol Biol Evol. 2012 Jan 19. PMID:22319152 doi:10.1093/molbev/mss015
  • Coquelle N, Talon R, Juers DH, Girard E, Kahn R, Madern D. Gradual Adaptive Changes of a Protein Facing High Salt Concentrations. J Mol Biol. 2010 Oct 1. PMID:20888835 doi:10.1016/j.jmb.2010.09.055
  • Fioravanti E, Vellieux FM, Amara P, Madern D, Weik M. Specific radiation damage to acidic residues and its relation to their chemical and structural environment. J Synchrotron Radiat. 2007 Jan;14(Pt 1):84-91. Epub 2006 Dec 15. PMID:17211074 doi:10.1107/S0909049506038623
  • Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccai G, Vellieux FM. The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J Mol Biol. 2003 Feb 21;326(3):859-73. PMID:12581646

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