Key role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar.
Abstract
The mechanism by which barnase and binase are stabilized in their complexes with barstar and the role of the Cys-40 residue of barstar in that stabilization have been investigated by scanning microcalorimetry. Melting of ribonuclease complexes with barstar and its Cys-82-Ala mutant is described by two 2-state transitions. The lower-temperature one corresponds to barstar denaturation and the higher-temperature transition to ribonuclease melting. The barstar mutation Cys-40-Ala, which is within the principal barnase-binding region of barstar, simplifies the melting to a single 2-state transition. The presence of residue Cys-40 in barstar results in additional stabilization of ribonuclease in the complex. Study holds ProTherm entries: 15000, 15001, 15002, 15003, 15004, 15005 Extra Details: DTT(1 mM) was added in the experiment barnase; binase; barstar mutant; protein-protein complex; thermal denaturation
Submission Details
ID: 2pwXrn4t3
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:45 p.m.
Version: 1
Publication Details
Protasevich II;Schulga AA;Vasilieva LI;Polyakov KM;Lobachov VM;Hartley RW;Kirpichnikov MP;Makarov AA,FEBS Lett. (1999) Key role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar. PMID:10094494Additional Information
Study Summary
Structure view and single mutant data analysis
Study data
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Data Distribution
Studies with similar sequences (approximate matches)