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1qmu

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Revision as of 11:39, 20 March 2008 by OCA (Talk | contribs)
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PDB ID 1qmu

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, resolution 2.70Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



DUCK CARBOXYPEPTIDASE D DOMAIN II


Overview

The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with overall topological similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This alpha/beta-hydrolase subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D.

About this Structure

1QMU is a Single protein structure of sequence from Anas specularioides. Full crystallographic information is available from OCA.

Reference

Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:10545093

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