1fye: Difference between revisions

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[[Image:1fye.gif|left|200px]]
{{Seed}}
[[Image:1fye.png|left|200px]]


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{{STRUCTURE_1fye|  PDB=1fye  |  SCENE=  }}  
{{STRUCTURE_1fye|  PDB=1fye  |  SCENE=  }}  


'''ASPARTYL DIPEPTIDASE (ANISOTROPIC B-FACTOR REFINEMENT)'''
===ASPARTYL DIPEPTIDASE (ANISOTROPIC B-FACTOR REFINEMENT)===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11106384}}, adds the Publication Abstract to the page
(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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