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Article

Crystallographic characterization of wild-type and mutant ribonuclease T1 complexes with several ribonucleotides.

Journal of biochemistry - 1 Nov 1990

Hakoshima T, Oka K, Toda S, Tanaka M, Goda K, Higo T, Itoh T, Minami H, Tomita K, Nishikawa S

Abstract excerpt

Ribonuclease T1 and the mutant enzymes were cocrystallized with several ribonucleotides, including non-hydrolyzable substrate analogs of di- and triribonucleotides, which have a novel guanylate in which the 2'-hydroxyl group of the ribose is replaced by a fluorine atom. One of the mutant enzymes has a tryptophan residue, instead of Tyr45 of the wild-type enzyme, to enhance the binding of ribonucleotides to the...

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PMID: 2081729
DOI: 10.1093/oxfordjournals.jbchem.a123265

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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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