2x0r: Difference between revisions

Revision as of 10:57, 12 May 2010

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2x0r, resolution 2.92Å ()

Ligands:

, ,

Activity:

Malate dehydrogenase, with EC number 1.1.1.37

Related:

2j5r, 2j5k, 1d3a, 2j5q, 2hlp, 1hlp, 1o6z

Structural annotation:
Resources:	InterPro : Ipr001557, Ipr016040, Ipr011275, Ipr015955, Ipr001236 Pfam : PF00056, PF02866

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

R207S,R292S MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)R207S,R292S MUTANT OF MALATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOARCULA MARISMORTUI (HOLO FORM)

Template:ABSTRACT PUBMED 12581646

About this StructureAbout this Structure

2X0R is a 2 chains structure with sequences from Haloarcula marismortui. This structure supersedes the now removed PDB entry 1gt2. Full crystallographic information is available from OCA.

ReferenceReference

^{[xtra 1]}^{[xtra 2]}^{[xtra 3]}^{[xtra 4]}^{[xtra 5]}^{[xtra 6]}

↑ 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

Page seeded by OCA on Wed May 12 10:57:13 2010

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OCA

[1] 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

[2] 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

[3] 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

[4] 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

[5] 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

[6] 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

[xtra 1]

[xtra 2]

[xtra 3]

[xtra 4]

[xtra 5]

[xtra 6]

@@ Line 20: / Line 20: @@
 ==About this Structure==
-X0R is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gt2 1gt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0R OCA].
+X0R is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gt2 1gt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0R OCA].
 ==Reference==
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 [[Category: Tricarboxylic acid cycle]]
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