2j5q
Template:ABSTRACT PUBMED 17211074

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2j5q, resolution 2.15Å () | |||||||||
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Ligands: | |||||||||
Activity: | Malate dehydrogenase, with EC number 1.1.1.37 | ||||||||
Related: | 1d3a, 1gt2, 1hlp, 1o6z, 2hlp, 2j5r, 2j5k | ||||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
2.15 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE FROM HALOARCULA MARISMORTUI AFTER FIRST RADIATION BURN (RADIATION DAMAGE SERIES)2.15 A RESOLUTION STRUCTURE OF THE WILD TYPE MALATE DEHYDROGENASE FROM HALOARCULA MARISMORTUI AFTER FIRST RADIATION BURN (RADIATION DAMAGE SERIES)
About this StructureAbout this Structure
2j5q 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 AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4]
- ↑ 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
- ↑ 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