1osj

STRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASESTRUCTURE OF 3-ISOPROPYLMALATE DEHYDROGENASE

Structural highlights 1osj is a 2 chain structure with sequence from Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LEU3_THET8] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01033] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of a thermostable Ala172Leu mutant, designated A172L, of 3-isopropylmalate dehydrogenase from Thermus thermophilus was determined. The crystal belongs to space group P2(1), with cell parameters a = 55.5 A, b = 88.1 A, c = 72.0 A and beta = 100.9 degrees. There is one dimer in each asymmetric unit. The final R factor is 17.8% with 69 water molecules at 2.35 A resolution. The mutation is located at the interface between domains and the C alpha trace of the mutant structure deviates from that of the native structure by as much as 1.7 A, while the structure of each domain barely changes. 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. The larger side chain at the mutated site contributed to the thermostability of the mutant protein by enhancing the local packing of side chains, and also by shifting the backbone of the opposing domain. A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase.,Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T Protein Eng. 1997 Jan;10(1):45-52. PMID:9051733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isopropylmalate dehydrogenase

spinqualitylabelsall models 1osj, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image