1qtr

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{{STRUCTURE_1qtr| PDB=1qtr | SCENE= }}
{{STRUCTURE_1qtr| PDB=1qtr | SCENE= }}
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'''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''
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===CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS===
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==Overview==
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Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.
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{{ABSTRACT_PUBMED_10467172}}
==About this Structure==
==About this Structure==
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[[Category: Prolyl aminopeptidase]]
[[Category: Prolyl aminopeptidase]]
[[Category: Serratia]]
[[Category: Serratia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:15:14 2008''

Revision as of 02:15, 29 July 2008

Image:1qtr.png

Template:STRUCTURE 1qtr

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

Template:ABSTRACT PUBMED 10467172

About this Structure

1QTR is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

Crystal structure of prolyl aminopeptidase from Serratia marcescens., Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K, J Biochem. 1999 Sep;126(3):559-65. PMID:10467172

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