1fy2

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{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
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'''ASPARTYL DIPEPTIDASE'''
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===ASPARTYL DIPEPTIDASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11106384 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11106384}}
==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Strand-helix motif]]
[[Category: Strand-helix motif]]
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Revision as of 01:06, 1 July 2008

Image:1fy2.png

Template:STRUCTURE 1fy2

ASPARTYL DIPEPTIDASE

Template:ABSTRACT PUBMED 11106384

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

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