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Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity.
- 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.
- Subjects :
- Amino Acid Substitution
Conserved Sequence
DNA chemistry
Endoribonucleases genetics
Escherichia coli genetics
Escherichia coli metabolism
Fungal Proteins genetics
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation
Protein Denaturation
Ribonucleotides chemistry
Spectrometry, Fluorescence
Substrate Specificity
Thermodynamics
Asparagine chemistry
Endoribonucleases chemistry
Endoribonucleases metabolism
Fungal Proteins chemistry
Fungal Proteins metabolism
Proteins chemistry
Subjects
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