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Article

Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution.

Biochemistry - 22 Feb 1994

Pletinckx J, Steyaert J, Zegers I, Choe H W, Heinemann U, Wyns L

Abstract excerpt

Glu58 is known to participate in phosphodiester transesterification catalyzed by the enzyme RNase T1. For Glu58 RNase T1, an altered mechanism has been proposed in which His40 replaces Glu58 as the base catalyst [Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P. (1990) Biochemistry 29, 9064-9072]. Glu58Ala Rnase T1 has been cocrystallized with guanosine 2'-monophosphate (2'-GMP). The crystals are of space...

Topics

Alanine
Binding Sites
Cations
Crystallization
Crystallography, X-Ray
Escherichia coli
Glutamates
Glutamic Acid
Guanosine Monophosphate
Hydrogen Bonding
Molecular Structure

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Conformation

Ribonuclease T1

Water

Source

Identifiers

PMID: 7906540
DOI: 10.1021/bi00173a006

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7906540-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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