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Dissecting histidine interactions of ribonuclease T 1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position 1 1Edited by A. R. Fersht

Autor: Stefan De Vos, Jan Steyaert, Ulrike Langhorst, Jan Doumen

Publikováno v: Journal of Molecular Biology. 275:651-661

His92 of Ribonuclease T1 combines functional and structural features involving both imidazole nitrogens. To evaluate the use of Asn and Gln substitutions in dissecting the properties of histidines, we analysed the consequences of the His92Gln and His

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1206c5426c3bfe5b5b98ae6b95453ac5
https://doi.org/10.1006/jmbi.1997.1480

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Dissection of the structural and functional role of a conserved hydration site in RNase T1

Autor: Dominique Maes, Ulrike Langhorst, Jan Steyaert, Jan Doumen, Patrice Roose, Bertil Halle, Vladimir P. Denisov, Remy Loris

Publikováno v: ResearcherID
Scopus-Elsevier

The reoccurrence of water molecules in crystal structures of RNase T1 was investigated. Five waters were found to be invariant in RNase T1 as well as in six other related fungal RNases. The structural, dynamical, and functional characteristics of one

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd1b626919b8fb6754ccb060b607d403
https://pubmed.ncbi.nlm.nih.gov/10211818

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Additivity of protein-guanine interactions in ribonuclease T1

Autor: Stefan Loverix, Jan Steyaert, Jan Doumen

Publikováno v: Vrije Universiteit Brussel

It has been established that Tyr-42, Tyr-45, and Glu-46 take part in a structural motif that renders guanine specificity to ribonuclease T1. We report on the impact of Tyr-42, Tyr-45, and Glu-46 substitutions on the guanine specificity of RNase T1. T

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f15c65e394b7deba9e407718c4592f42
https://pubmed.ncbi.nlm.nih.gov/9092491

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A catalytic function for the structurally conserved residue Phe 100 of ribonuclease T1

Autor: Malgorzata Gonciarz, Remy Loris, Ingrid Zegers, Jan Doumen, Jan Steyaert, Lode Wyns

Publikováno v: Scopus-Elsevier

The function of the conserved Phe 100 residue of RNase T1 (EC 3.1.27.3) has been investigated by site-directed mutagenesis and X-ray crystallography. Replacement of Phe 100 by alanine results in a mutant enzyme with kcat reduced 75-fold and a small i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d1fb2d3329440ae0be3a88a979b79a
https://pubmed.ncbi.nlm.nih.gov/8844843

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A catalytic function of the structurally conserved Phe100 in ribonuclease T1

Autor: Jan Doumen, Magorzata Gonciarz, Ingrid Zegers, Remy Loris, Lode Wyns, Jan Steyaert

Publikováno v: Vrije Universiteit Brussel

The function of the conserved Phe 100 residue of RNase TI (EC 3.1.27.3) has been investigated by site-directed mutagenesis and X-ray crystallography. Replacement of Phe 100 by alanine results in a mutant enzyme with kc,, reduced 75-fold and a small i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::c7da02822ce2c406a19018d92061d95b
https://researchportal.vub.be/en/publications/84b1690b-25d5-4551-b099-340270b20a6e

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