1qmu: Difference between revisions

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.

1QMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_specularioides Anas specularioides] with SO4 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: ZN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QMU OCA].  

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