1BGS

RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR

Summary for 1BGS

• Entry DOI: 10.2210/pdb1bgs/pdb
• Descriptor: BARNASE, BARSTAR (3 entities in total)
• Functional Keywords: endonuclease
• Biological source: Bacillus amyloliquefaciens; More
• Cellular location: Secreted: P00648; Cytoplasm: P11540
• Total number of polymer chains: 6
• Total formula weight: 67668.40

Authors

Guillet, V.,Lapthorn, A.,Mauguen, Y. (deposition date: 1993-11-02, release date: 1994-04-30, Last modification date: 2024-02-07)

Primary citation

Guillet, V.,Lapthorn, A.,Hartley, R.W.,Mauguen, Y.
Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.
Structure, 1:165-176, 1993

PubMed Abstract: Protein-protein recognition is fundamental to most biological processes. The information we have so far on the interfaces between proteins comes largely from several protease-inhibitor and antigen-antibody complexes. Barnase, a bacterial ribonuclease, and barstar, its natural inhibitor, form a tight complex which provides a good model for the study and design of protein-protein non-covalent interactions.

PubMed: 16100951
DOI: 10.1016/0969-2126(93)90018-C

Experimental method

X-RAY DIFFRACTION (2.6 Å)