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Article

Proposal for new catalytic roles for two invariant residues in Escherichia coli ribonuclease HI.

Protein engineering - 1 Oct 1996

Kashiwagi T, Jeanteur D, Haruki M, Katayanagi K, Kanaya S, Morikawa K

Abstract excerpt

Three mutants of Escherichia coli ribonuclease HI, in which an invariant acidic residue Asp134 was replaced, were crystallized, and their three-dimensional structures were determined by X-ray crystallography. The D134A mutant is completely inactive, whereas the other two mutants, D134H and D134N, retain 59 and 90% activities relative to the wild-type, respectively. The overall structures of these three mutant...

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Source

Identifiers

PMID: 8931125
DOI: 10.1093/protein/9.10.857

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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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