1oyv: Difference between revisions

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[[Image:1oyv.jpg|left|200px]]
[[Image:1oyv.jpg|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span>
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{{STRUCTURE_1oyv| PDB=1oyv  | SCENE= }}  
|RELATEDENTRY=[[1scn|1SCN]], [[4sgb|4SGB]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyv OCA], [http://www.ebi.ac.uk/pdbsum/1oyv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oyv RCSB]</span>
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'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''
'''Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg'''
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[[Category: Pearce, G.]]
[[Category: Pearce, G.]]
[[Category: Ryan, C A.]]
[[Category: Ryan, C A.]]
[[Category: multidomain inhibitor]]
[[Category: Multidomain inhibitor]]
[[Category: potato ii family]]
[[Category: Potato ii family]]
[[Category: serine proteinase inhibitor]]
[[Category: Serine proteinase inhibitor]]
[[Category: ternary complex]]
[[Category: Ternary complex]]
 
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Revision as of 04:26, 3 May 2008

File:1oyv.jpg

Template:STRUCTURE 1oyv

Crystal structure of tomato inhibitor-II in a ternary complex with subtilisin Carlsberg


OverviewOverview

Multidomain proteinase inhibitors play critical roles in the defense of plants against predation by a wide range of pests. Despite a wealth of structural information on proteinase-single domain inhibitor interactions, the structural basis of inhibition by multidomain proteinase inhibitors remains poorly understood. Here we report the 2.5-A resolution crystal structure of the two-headed tomato inhibitor-II (TI-II) in complex with two molecules of subtilisin Carlsberg; it reveals how a multidomain inhibitor from the Potato II family of proteinase inhibitors can bind to and simultaneously inhibit two enzyme molecules within a single ternary complex. The N terminus of TI-II initiates the folding of Domain I (Lys-1 to Cys-15 and Pro-84 to Met-123) and then completes Domain II (Ile-26 to Pro-74) before coming back to complete the rest of Domain I (Pro-84 to Met-123). The two domains of TI-II adopt a similar fold and are arranged in an extended configuration that presents two reactive site loops at the opposite ends of the inhibitor molecule. Each subtilisin molecule interacts with a reactive site loop of TI-II through the standard, canonical binding mode. Remarkably, a significant distortion of the active site of subtilisin is induced by the presence of phenylalanine in the P1 position of reactive site loop II of TI-II. The structure of the TI-II.(subtilisin)2 complex provides a molecular framework for understanding how multiple inhibitory domains in a single Potato II type proteinase inhibitor molecule from the Potato II family act to inhibit proteolytic enzymes.

About this StructureAbout this Structure

1OYV is a Protein complex structure of sequences from Bacillus licheniformis and Solanum lycopersicum. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of inhibition revealed by a 1:2 complex of the two-headed tomato inhibitor-II and subtilisin Carlsberg., Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ryan CA, James MN, J Biol Chem. 2003 Jun 27;278(26):24062-71. Epub 2003 Apr 8. PMID:12684499 Page seeded by OCA on Sat May 3 04:26:51 2008

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