2c1c

From Proteopedia

Revision as of 14:49, 30 October 2007

STRUCTURAL BASIS OF THE RESISTANCE OF AN INSECT CARBOXYPEPTIDASE TO PLANT PROTEASE INHIBITORS

Overview

Corn earworm (Helicoverpa zea), also called tomato fruitworm, is a common, pest of many Solanaceous plants. This insect is known to adapt to the, ingestion of plant serine protease inhibitors by using digestive proteases, that are insensitive to inhibition. We have now identified a B-type, carboxypeptidase of H. zea (CPBHz) insensitive to potato carboxypeptidase, inhibitor (PCI) in corn earworm. To elucidate the structural features, leading to the adaptation of the insect enzyme, the crystal structure of, the recombinant CPBHz protein was determined by x-ray diffraction. CPBHz, is a member of the A/B subfamily of metallocarboxypeptidases, which, displays the characteristic metallocarboxypeptidase alpha/beta-hydrolase, fold, and does not differ essentially from the previously described, ... [(full description)]

About this Structure

2C1C is a [Single protein] structure of sequence from [Helicoverpa zea] with ZN and Y1 as [ligands]. Active as [Carboxypeptidase B], with EC number [3.4.17.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors., Bayes A, Comellas-Bigler M, Rodriguez de la Vega M, Maskos K, Bode W, Aviles FX, Jongsma MA, Beekwilder J, Vendrell J, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16602-7. Epub 2005 Oct 31. PMID:16260742

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