1jqg

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[[Image:1jqg.jpg|left|200px]]<br /><applet load="1jqg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jqg.jpg|left|200px]]
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caption="1jqg, resolution 2.5&Aring;" />
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'''Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera'''<br />
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{{Structure
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|PDB= 1jqg |SIZE=350|CAPTION= <scene name='initialview01'>1jqg</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1]
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|GENE=
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}}
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'''Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JQG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicoverpa_armigera Helicoverpa armigera] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQG OCA].
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1JQG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicoverpa_armigera Helicoverpa armigera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQG OCA].
==Reference==
==Reference==
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Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera., Estebanez-Perpina E, Bayes A, Vendrell J, Jongsma MA, Bown DP, Gatehouse JA, Huber R, Bode W, Aviles FX, Reverter D, J Mol Biol. 2001 Oct 26;313(3):629-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11676544 11676544]
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Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera., Estebanez-Perpina E, Bayes A, Vendrell J, Jongsma MA, Bown DP, Gatehouse JA, Huber R, Bode W, Aviles FX, Reverter D, J Mol Biol. 2001 Oct 26;313(3):629-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11676544 11676544]
[[Category: Carboxypeptidase A]]
[[Category: Carboxypeptidase A]]
[[Category: Helicoverpa armigera]]
[[Category: Helicoverpa armigera]]
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[[Category: pro-protein]]
[[Category: pro-protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:03 2008''

Revision as of 10:07, 20 March 2008


PDB ID 1jqg

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands:
Activity: Carboxypeptidase A, with EC number 3.4.17.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera


Overview

The cotton bollworm Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae) is one of the most serious insect pests in Australia, India and China. The larva causes substantial economical losses to legume, fibre, cereal oilseed and vegetable crops. This pest has proven to be difficult to control by conventional means, mainly due to the development of pesticide resistance. We present here the 2.5 A crystal structure from the novel procarboxypeptidase (PCPAHa) found in the gut extracts from H. armigera larvae, the first one reported for an insect. This metalloprotease is synthesized as a zymogen of 46.6 kDa which, upon in vitro activation with Lys-C endoproteinase, yields a pro-segment of 91 residues and an active carboxypeptidase moiety of 318 residues. Both regions show a three-dimensional structure quite similar to the corresponding structures in mammalian digestive carboxypeptidases, the most relevant structural differences being located in the loops between conserved secondary structure elements, including the primary activation site. This activation site contains the motif (Ala)(5)Lys at the C terminus of the helix connecting the pro- and the carboxypeptidase domains. A remarkable feature of PCPAHa is the occurrence of the same (Ala)(6)Lys near the C terminus of the active enzyme. The presence of Ser255 in PCPAHa instead of Ile and Asp found in the pancreatic A and B forms, respectively, enlarges the S1' specificity pocket and influences the substrate preferences of the enzyme. The C-terminal tail of the leech carboxypeptidase inhibitor has been modelled into the PCPAHa active site to explore the substrate preferences and the enzymatic mechanism of this enzyme.

About this Structure

1JQG is a Single protein structure of sequence from Helicoverpa armigera. Full crystallographic information is available from OCA.

Reference

Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera., Estebanez-Perpina E, Bayes A, Vendrell J, Jongsma MA, Bown DP, Gatehouse JA, Huber R, Bode W, Aviles FX, Reverter D, J Mol Biol. 2001 Oct 26;313(3):629-38. PMID:11676544

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