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Article

A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase.

Protein engineering - 1 Jan 1997

Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T

Abstract excerpt

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...

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Identifiers

PMID: 9051733
DOI: 10.1093/protein/10.1.45

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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