1qtr

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[[Image:1qtr.jpg|left|200px]]
[[Image:1qtr.jpg|left|200px]]
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{{Structure
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|PDB= 1qtr |SIZE=350|CAPTION= <scene name='initialview01'>1qtr</scene>, resolution 2.32&Aring;
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The line below this paragraph, containing "STRUCTURE_1qtr", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span>
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{{STRUCTURE_1qtr| PDB=1qtr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtr OCA], [http://www.ebi.ac.uk/pdbsum/1qtr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qtr RCSB]</span>
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'''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''
'''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''
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[[Category: Uchikawa, K.]]
[[Category: Uchikawa, K.]]
[[Category: Yoshimoto, T.]]
[[Category: Yoshimoto, T.]]
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[[Category: alpha beta hydrolase fold]]
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[[Category: Alpha beta hydrolase fold]]
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[[Category: iminopeptidase]]
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[[Category: Iminopeptidase]]
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[[Category: proline]]
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[[Category: Proline]]
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[[Category: prolyl aminopeptidase]]
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[[Category: Prolyl aminopeptidase]]
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[[Category: serratia]]
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[[Category: Serratia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:53 2008''
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Revision as of 03:41, 3 May 2008

Template:STRUCTURE 1qtr

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS


Overview

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.

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 Page seeded by OCA on Sat May 3 06:41:45 2008

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