Motion in 3-Isopropylmalate Dehydrogenase [ipdh]

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Classification [D-h-2]

Structures
1IPD [ PartsList ]
1OSJ [ PartsList ]

Description
Motion is due to engineered mutations, but thought to be indicative of actual enzyme function. From the abstract to Qu et al. (Protein Eng 1997 Jan;10(1):45-52): "The mutant enzyme has a more closed conformation compared with the wild-type enzyme as a result of the replacement of Ala with Leu at residue 172. These structural variations were found independent of the crystal packing, because the structure of wild type was the same in crystals obtained in different precipitants. The hinge regions for the movement of domains are located around the active cleft of the enzyme, an observation that implies that the mobility of domains around the hinge is indispensable for the activity of the enzyme."

References
C Qu, S Akanuma, H Moriyama, N Tanaka, T Oshima (1997). A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase. Protein Eng, 10:45-52 [Medline info for 9051733]
K Imada, M Sato, N Tanaka, Y Katsube, Y Matsuura, T Oshima (1991). Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 A resolution. J Mol Biol, 222:725-38 [Medline info for 1748999]

GO terms associated with structures
Molecular functionoxidoreductase activity, 3-isopropylmalate dehydrogenase activity
Cellular componentcytoplasm
Biological processmetabolism, leucine biosynthesis

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
3-Isopropylmalate Dehydrogenas 1ipd [ A ] 1osj [ A ] 345



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu