1bgs

<table><tr><td colspan='2'>[[1bgs]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BGS FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgs OCA], [http://pdbe.org/1bgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bgs RCSB], [http://www.ebi.ac.uk/pdbsum/1bgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgs ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM]] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. [[http://www.uniprot.org/uniprot/BARS_BACAM BARS_BACAM]] Inhibitor of the ribonuclease barnase. Forms a one-to-one non-covalent complex.

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== Publication Abstract from PubMed ==

BACKGROUND: 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. RESULTS: Here we report the structure of a complex between barnase and a fully functional mutant of barstar determined by X-ray analysis. Barstar is composed of three parallel alpha-helices stacked against a three-stranded parallel, beta-sheet, and sterically blocks the active site of the enzyme with an alpha-helix and adjacent loop. The buried surface in the interface between the two molecules totals 1630 A2. The barnase-barstar complex is predominantly stabilized by charge interactions involving positive charges in the active site of the enzyme. Asp39 of barstar binds to the phosphate-binding site of barnase, mimicking enzyme-substrate interactions. CONCLUSION: The phosphate-binding site of the enzyme is the anchor point for inhibitor binding. We propose that this is also likely to be the case for other ribonuclease inhibitors.

Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.,Guillet V, Lapthorn A, Hartley RW, Mauguen Y Structure. 1993 Nov 15;1(3):165-76. PMID:16100951<ref>PMID:16100951</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Ribonuclease|Ribonuclease]]

[[Category: Guillet, V]]

[[Category: Lapthorn, A]]

[[Category: Mauguen, Y]]

[[Category: Endonuclease]]