1fy2
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(New page: 200px<br /><applet load="1fy2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy2, resolution 1.2Å" /> '''ASPARTYL DIPEPTIDASE'...)
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Revision as of 13:20, 20 November 2007
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ASPARTYL DIPEPTIDASE
Overview
The three-dimensional structure of Salmonella typhimurium aspartyl, dipeptidase, peptidase E, was solved crystallographically and refined to, 1.2-A resolution. The structure of this 25-kDa enzyme consists of two, mixed beta-sheets forming a V, flanked by six alpha-helices. The active, site contains a Ser-His-Glu catalytic triad and is the first example of a, serine peptidase/protease with a glutamate in the catalytic triad. The, active site Ser is located on a strand-helix motif reminiscent of that, found in alpha/beta-hydrolases, but the polypeptide fold and the, organization of the catalytic triad differ from those of the known serine, proteases. This enzyme is a member of a family of serine hydrolases and, appears to represent a new example of convergent evolution of peptidase, activity.
About this Structure
1FY2 is a Single protein structure of sequence from Salmonella typhimurium with CD as ligand. Full crystallographic information is available from OCA.
Reference
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad., Hakansson K, Wang AH, Miller CG, Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384
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