1o6z
From Proteopedia
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===1.95 A RESOLUTION STRUCTURE OF (R207S,R292S) MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)=== | ===1.95 A RESOLUTION STRUCTURE OF (R207S,R292S) MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)=== | ||
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Revision as of 13:34, 27 July 2012
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| 1o6z, resolution 1.95Å () | |||||||||
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| Ligands: | , | ||||||||
| Activity: | Malate dehydrogenase, with EC number 1.1.1.37 | ||||||||
| Related: | 1d3a, 1gt2, 1hlp, 2hlp | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
1.95 A RESOLUTION STRUCTURE OF (R207S,R292S) MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)
Template:ABSTRACT PUBMED 12581646
About this Structure
1o6z is a 4 chain structure of Johnson sandbox 1 and Malate dehydrogenase with sequence from Haloarcula marismortui. Full crystallographic information is available from OCA.
See Also
Reference
- 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
- Madern D, Ebel C, Mevarech M, Richard SB, Pfister C, Zaccai G. Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. Biochemistry. 2000 Feb 8;39(5):1001-10. PMID:10653644
- Richard SB, Madern D, Garcin E, Zaccai G. Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry. 2000 Feb 8;39(5):992-1000. PMID:10653643
- Dym O, Mevarech M, Sussman JL. Structural Features That Stabilize Halophilic Malate Dehydrogenase from an Archaebacterium. Science. 1995 Mar 3;267(5202):1344-1346. PMID:17812611 doi:267/5202/1344
- Madern D, Pfister C, Zaccai G. Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Eur J Biochem. 1995 Jun 15;230(3):1088-95. PMID:7601139
- Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M. Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry. 1993 Apr 27;32(16):4308-13. PMID:8476859
