2x0r: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2x0r.png|left|200px]] | [[Image:2x0r.png|left|200px]] | ||
| Line 20: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
[[2x0r]] is a 2 chain structure of [[Malate dehydrogenase]] with sequence 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]. | |||
==See Also== | |||
*[[Malate dehydrogenase]] | |||
==Reference== | ==Reference== | ||
| Line 38: | Line 40: | ||
[[Category: Protein-solvent interaction]] | [[Category: Protein-solvent interaction]] | ||
[[Category: Tricarboxylic acid cycle]] | [[Category: Tricarboxylic acid cycle]] | ||
Revision as of 00:57, 15 March 2011
| |||||||||
| 2x0r, resolution 2.92Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||||
| Activity: | Malate dehydrogenase, with EC number 1.1.1.37 | ||||||||
| Related: | 2j5r, 2j5k, 1d3a, 2j5q, 2hlp, 1hlp, 1o6z | ||||||||
| |||||||||
| |||||||||
| 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 chain structure of Malate dehydrogenase with sequence from Haloarcula marismortui. This structure supersedes the now removed PDB entry 1gt2. Full crystallographic information is available from OCA.
See AlsoSee Also
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