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Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity.

Authors :
Siemer A
Masip M
Carreras N
García-Ortega L
Oñaderra M
Bruix M
Del Pozo AM
Gavilanes JG
Source :
Biological chemistry [Biol Chem] 2004 Dec; Vol. 385 (12), pp. 1165-70.
Publication Year :
2004

Abstract

Asparagine 54 of alpha-sarcin is a conserved residue within the proteins of the ribotoxin family of microbial ribonucleases. It is located in loop 2 of the protein, which lacks repetitive secondary structure elements but exhibits a well-defined conformation. Five mutant variants at this residue have been produced and characterized. The spectroscopic characterization of these proteins indicates that the overall conformation is not changed upon mutation. Activity and denaturation assays show that Asn-54 largely contributes to protein stability, and its presence is a requirement for the highly specific inhibitory activity of these ribotoxins on ribosomes.

Details

Language :
English
ISSN :
1431-6730
Volume :
385
Issue :
12
Database :
MEDLINE
Journal :
Biological chemistry
Publication Type :
Academic Journal
Accession number :
15653429
Full Text :
https://doi.org/10.1515/BC.2004.150