Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity
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Ansgar Siemer
, Manuel Masip , Nelson Carreras , Lucía García-Ortega , Mercedes Oñaderra , Marta Bruix , Álvaro Martínez del Pozo and José G. Gavilanes
Abstract
Asparagine 54 of α-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.
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©2004 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Structural flexibility of small GTPases. Can it explain their functional versatility?
- Neuroendocrine regulation of salivary IgA synthesis and secretion: implications for oral health
- Structural characterization of extracellular lipase from Streptomyces rimosus: assignment of disulfide bridge pattern by mass spectrometry
- Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy
- Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity
- Replacement of the interchain disulfide bridge-forming amino acids A7 and B7 by glutamate impairs the structure and activity of insulin
- Stereospecificity of horseradish peroxidase
- Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1α and yeast alcohol dehydrogenase
- Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase
- St. John's wort (Hypericum perforatum) counteracts cytokine-induced tryptophan catabolism in vitro
- Nuclear fibroblast growth factor-2 interacts specifically with splicing factor SF3a66
- Content Index
- Author Index
- Subject Index
Articles in the same Issue
- Structural flexibility of small GTPases. Can it explain their functional versatility?
- Neuroendocrine regulation of salivary IgA synthesis and secretion: implications for oral health
- Structural characterization of extracellular lipase from Streptomyces rimosus: assignment of disulfide bridge pattern by mass spectrometry
- Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy
- Conserved asparagine residue 54 of α-sarcin plays a role in protein stability and enzyme activity
- Replacement of the interchain disulfide bridge-forming amino acids A7 and B7 by glutamate impairs the structure and activity of insulin
- Stereospecificity of horseradish peroxidase
- Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1α and yeast alcohol dehydrogenase
- Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase
- St. John's wort (Hypericum perforatum) counteracts cytokine-induced tryptophan catabolism in vitro
- Nuclear fibroblast growth factor-2 interacts specifically with splicing factor SF3a66
- Content Index
- Author Index
- Subject Index