1pju

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[[Image:1pju.jpg|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1oyv|1OYV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pju OCA], [http://www.ebi.ac.uk/pdbsum/1pju PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pju RCSB]</span>
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'''Unbound form of Tomato Inhibitor-II'''
'''Unbound form of Tomato Inhibitor-II'''
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[[Category: Pearce, G.]]
[[Category: Pearce, G.]]
[[Category: Ryan, C A.]]
[[Category: Ryan, C A.]]
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[[Category: proteinase inhibitor]]
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[[Category: Proteinase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:10:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:39 2008''
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Revision as of 02:10, 3 May 2008

Template:STRUCTURE 1pju

Unbound form of Tomato Inhibitor-II


Overview

The Potato II (Pot II) family of proteinase inhibitors plays important roles in the constitutive and inducible defense of plants against predation by a wide range of pests. The structural basis of inhibition by a multidomain Pot II family inhibitor was revealed recently by the structure of the ternary complex between the two-headed tomato inhibitor-II (TI-II) and two molecules of subtilisin Carlsberg. Here we report the 2.15-A resolution crystal structure of the unbound form of TI-II that reveals significant conformational flexibility in the absence of bound proteinase molecules. The four independent copies of unbound TI-II in the asymmetric unit of the unit cell display a range of different conformations when compared with the bound form of the inhibitor, most strikingly in the orientations of the inhibitory domains and in the conformations of the reactive site loops. One of the two linker segments (residues 74 to 79) between the two domains as well as the adjacent beta-strand in Domain I (residues 80-85) is well ordered in all four copies of the unbound inhibitor, even though this region appeared to be disordered in the structure of the ternary complex. Conformational flexibility seen in the reactive site loops of unbound TI-II suggests a mechanism by which the inhibitor can balance the need for tight binding with the need for broad inhibitory function.

About this Structure

1PJU is a Single protein structure of sequence from Solanum lycopersicum. Full crystallographic information is available from OCA.

Reference

Unbound form of tomato inhibitor-II reveals interdomain flexibility and conformational variability in the reactive site loops., Barrette-Ng IH, Ng KK, Cherney MM, Pearce G, Ghani U, Ryan CA, James MN, J Biol Chem. 2003 Aug 15;278(33):31391-400. Epub 2003 Jun 4. PMID:12788916 Page seeded by OCA on Sat May 3 05:10:03 2008

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