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Structure paper

TitleHalophilic 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.
Journal, issue, pagesBiochemistry, Vol. 39, Page 992-1000, Year 2000
Publish dateSep 28, 1999 (structure data deposition date)
AuthorsRichard, S.B. / Madern, D. / Garcin, E. / Zaccai, G.
External linksBiochemistry / PubMed:10653643
MethodsX-ray diffraction
Resolution2.59 - 2.94 Å
Structure data

PDB-1d3a:
CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM
Method: X-RAY DIFFRACTION / Resolution: 2.94 Å

PDB-2hlp:
CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • haloarcula marismortui (Halophile)
KeywordsOXIDOREDUCTASE / ROSSMANN FOLD AND 3 SORTS OF COMPLEX SALT BRIDGES / HALOPHILIC / ION-BINDING / SALT BRIDGES / MALATE DEHYDROGENASE

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