Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: An internal reprieve tolerance mechanism

Masahiro Sakurai, Masato Ohzeki, Kentaro Miyazaki, Hideaki Moriyama, Mamoru Sato, Nobuo Tanaka, Tairo Oshima

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)124-128
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume52
Issue number1
DOIs
StatePublished - Jan 1 1996

ASJC Scopus subject areas

  • Structural Biology

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