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Article

Structural and thermodynamic analyses of Escherichia coli RNase HI variant with quintuple thermostabilizing mutations.

The FEBS journal - 1 Nov 2007

Haruki Mitsuru, Tanaka Masaki, Motegi Takehiko, Tadokoro Takashi, Koga Yuichi, Takano Kazufumi, Kanaya Shigenori

Abstract excerpt

A combination of five thermostabilizing mutations, Gly23-->Ala, His62-->Pro, Val74-->Leu, Lys95-->Gly, and Asp134-->His, has been shown to additively enhance the thermostability of Escherichia coli RNase HI [Akasako A, Haruki M, Oobatake M & Kanaya S (1995) Biochemistry34, 8115-8122]. In this study, we determined the crystal structure of the protein with these mutations (5H-RNase HI) to analyze the effects of the...

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Identifiers

PMID: 17944939
DOI: 10.1111/j.1742-4658.2007.06104.x

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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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