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1wm1

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[[Image:1wm1.jpg|left|200px]]
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{{STRUCTURE_1wm1| PDB=1wm1 | SCENE= }}
{{STRUCTURE_1wm1| PDB=1wm1 | SCENE= }}
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'''Crystal Structure of Prolyl Aminopeptidase, Complex with Pro-TBODA'''
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===Crystal Structure of Prolyl Aminopeptidase, Complex with Pro-TBODA===
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==Overview==
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Prolyl aminopeptidase from Serratia marcescens hydrolyzed x-beta-naphthylamides (x=prolyl, alanyl, sarcosinyl, L-alpha-aminobutylyl, and norvalyl), which suggested that the enzyme has a pocket for a five-member ring. Based on the substrate specificity, novel inhibitors of Pro, Ala, and Sar having 2-tert-butyl-[1,3,4]oxadiazole (TBODA) were synthesized. The K(i) value of Pro-TBODA, Ala-TBODA, and Sar-TBODA was 0.5 microM, 1.6 microM, and 12mM, respectively. The crystal structure of enzyme-Pro-TBODA complex was determined. Pro-TBODA was located at the active site. Four electrostatic interactions were located between the enzyme and the amino group of Pro inhibitors (Glu204:0E1-N:Inh, Glu204:0E2-N:Inh, Glu232:0E1-N:Inh, and Gly46:O-N:Inh), and the residue of the inhibitors was inserted into the hydrophobic pocket composed of Phe139, Leu141, Leu146, Tyr149, Tyr150, and Phe236. The roles of Phe139, Tyr149, and Phe236 in the hydrophobic pocket and Glu204 and Glu232 in the electrostatic interactions were confirmed by site-directed mutagenesis, which indicated that the molecular recognition of proline is achieved through four electrostatic interactions and an insertion in the hydrophobic pocket of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 12893291 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12893291}}
==About this Structure==
==About this Structure==
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[[Category: Complex with inhibitor]]
[[Category: Complex with inhibitor]]
[[Category: Proline iminopeptidase]]
[[Category: Proline iminopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:51:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:22:38 2008''

Revision as of 11:22, 29 July 2008

Image:1wm1.png

Template:STRUCTURE 1wm1

Crystal Structure of Prolyl Aminopeptidase, Complex with Pro-TBODA

Template:ABSTRACT PUBMED 12893291

About this Structure

1WM1 is a Single protein structure of sequence from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor., Inoue T, Ito K, Tozaka T, Hatakeyama S, Tanaka N, Nakamura KT, Yoshimoto T, Arch Biochem Biophys. 2003 Aug 15;416(2):147-54. PMID:12893291

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