1qfm | pdb_00001qfm

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Revision as of 22:31, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1qfm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfm, resolution 1.400Å" /> '''PROLYL OLIGOPEPTIDA...)
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File:1qfm.jpg


1qfm, resolution 1.400Å

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PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE

Overview

Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new, class of serine peptidases. The enzyme is involved in the maturation and, degradation of peptide hormones and neuropeptides, which relate to the, induction of amnesia. The 1.4 A resolution crystal structure is presented, here. The enzyme contains a peptidase domain with an alpha/beta hydrolase, fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the, central tunnel of an unusual beta propeller. This domain makes prolyl, oligopeptidase an oligopeptidase by excluding large structured peptides, from the active site. In this way, the propeller protects larger peptides, and proteins from proteolysis in the cytosol. The structure is also, obtained with a transition state inhibitor, which may facilitate drug, design to treat memory disorders.

About this Structure

1QFM is a Single protein structure of sequence from Sus scrofa with SGL, SGM and GOL as ligands. Active as Prolyl oligopeptidase, with EC number 3.4.21.26 Full crystallographic information is available from OCA.

Reference

Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis., Fulop V, Bocskei Z, Polgar L, Cell. 1998 Jul 24;94(2):161-70. PMID:9695945

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