Recognition of RNase Sa by the inhibitor barstar: structure of the complex at 1.7 A resolution.

Crystal structure of the complex RNase Sa-barstar at 1.7 A resolution.

A Continuum Electrostatic Analysis of Protein Binding: Barnase–Barstar Complex Formation

Understanding the nature of protein–protein recognition is fundamental to the study of biological processes. The complex between barnase, a bacterial RNase, with its intracellular inhibitor, barstar, is a suitable system for the general problem of molecular recognition since the structures of the proteins have been solved, both separately and in the protein complex. This interaction between bar...

Protein-protein interaction: a genetic selection for compensating mutations at the barnase-barstar interface.

Barnase and barstar are trivial names of the extracellular RNase and its intracellular inhibitor produced by Bacillus amyloliquefaciens. Inhibition involves the formation of a very tight one-to-one complex of the two proteins. With the crystallographic solution of the structure of the barnase-barstar complex and the development of methods for measuring the free energy of binding, the pair can b...

Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7 A resolution.

The crystal structure of a complex of ribonuclease from Streptomyces aureofaciens (RNase Sa) with guanosine-2'-monophosphate (2'-GMP) has been refined against synchrotron data recorded from a single crystal using radiation from beamline X31 at EMBL, Hamburg, and an imaging plate scanner. The crystals are in space group P2(1)2(1)2(1) with cell dimensions a = 64.7, b = 78.8 and c = 39.1 A. The st...

Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution.

We have solved, refined, and analyzed the 2.0-å resolution crystal structure of a 1:1 complex between the bacterial ribonuclease, barnase, and a Cys-->Ala(40,82) double mutant of its intracellular polypeptide inhibitor, barstar. Barstar inhibits barnase by sterically blocking the active site with a helix and adjacent loop segment. Almost half of the 14 hydrogen bonds between barnase and barstar...