1gv0
STRUCTURAL BASIS FOR THERMOPHILIC PROTEIN STABILITY: STRUCTURES OF THERMOPHILIC AND MESOPHILIC MALATE DEHYDROGENASES
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OverviewOverview
The three-dimensional structure of four malate dehydrogenases (MDH) from, thermophilic and mesophilic phototropic bacteria have been determined by, X-ray crystallography and the corresponding structures compared. In, contrast to the dimeric quaternary structure of most MDHs, these MDHs are, tetramers and are structurally related to tetrameric malate dehydrogenases, from Archaea and to lactate dehydrogenases. The tetramers are dimers of, dimers, where the structures of each subunit and the dimers are similar to, the dimeric malate dehydrogenases. The difference in optimal growth, temperature of the corresponding organisms is relatively small, ranging, from 32 to 55 degrees C. Nevertheless, on the basis of the four crystal, structures, a number of factors that are likely to contribute to ... [(full description)]
About this StructureAbout this Structure
1GV0 is a [Single protein] structure of sequence from [Chlorobaculum tepidum] with NAD as [ligand]. Active as [Malate dehydrogenase], with EC number [1.1.1.37]. Structure known Active Site: NAA. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases., Dalhus B, Saarinen M, Sauer UH, Eklund P, Johansson K, Karlsson A, Ramaswamy S, Bjork A, Synstad B, Naterstad K, Sirevag R, Eklund H, J Mol Biol. 2002 May 3;318(3):707-21. PMID:12054817
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