1fy2
From Proteopedia
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'''ASPARTYL DIPEPTIDASE''' | '''ASPARTYL DIPEPTIDASE''' | ||
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[[Category: Miller, C G.]] | [[Category: Miller, C G.]] | ||
[[Category: Wang, A H.J.]] | [[Category: Wang, A H.J.]] | ||
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| - | [[Category: | + | [[Category: Serine protease]] |
| - | [[Category: | + | [[Category: Strand-helix motif]] |
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Revision as of 13:53, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 16:53:36 2008
