Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IDM

3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

Summary for 1IDM
Entry DOI10.2210/pdb1idm/pdb
Descriptor3-ISOPROPYLMALATE DEHYDROGENASE (2 entities in total)
Functional Keywordschimera, oxidoreductase
Biological sourceThermus thermophilus
Cellular locationCytoplasm: P00351
Total number of polymer chains1
Total formula weight36471.66
Authors
Sakurai, M.,Ohzeki, M.,Moriyama, H.,Sato, M.,Tanaka, N. (deposition date: 1995-05-19, release date: 1995-09-15, Last modification date: 2024-02-07)
Primary citationSakurai, M.,Ohzeki, M.,Miyazaki, K.,Moriyama, H.,Sato, M.,Tanaka, N.,Oshima, T.
Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism.
Acta Crystallogr.,Sect.D, 52:124-128, 1996
Cited by
PubMed Abstract: A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus thermophilus was constructed to investigate the relationship between the flexibility of the structure and the thermostability of the enzyme. The structure of the mutant enzyme was determined by X-ray crystallography and was found to be almost the same as that of the native enzyme with a reduced temperature factor. Although the mutant protein had lost the flexible loop, its function and thermostability had remained unchanged. This phenomenon can be explained by an internal reprieve tolerance mechanism.
PubMed: 15299733
DOI: 10.1107/S0907444995007190
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon