1bgs
From Proteopedia
(New page: 200px<br /><applet load="1bgs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bgs, resolution 2.6Å" /> '''RECOGNITION BETWEEN A...) |
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| - | [[Image:1bgs.jpg|left|200px]]<br /><applet load="1bgs" size=" | + | [[Image:1bgs.jpg|left|200px]]<br /><applet load="1bgs" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bgs, resolution 2.6Å" /> | caption="1bgs, resolution 2.6Å" /> | ||
'''RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR'''<br /> | '''RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Protein-protein recognition is fundamental to most biological | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BGS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http:// | + | 1BGS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: endonuclease]] | [[Category: endonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:06 2008'' |
Revision as of 09:55, 21 February 2008
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RECOGNITION BETWEEN A BACTERIAL RIBONUCLEASE, BARNASE, AND ITS NATURAL INHIBITOR, BARSTAR
Overview
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.
About this Structure
1BGS is a Protein complex structure of sequences from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.
Reference
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
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