1erz

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[[Image:1erz.gif|left|200px]]
[[Image:1erz.gif|left|200px]]
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{{Structure
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|PDB= 1erz |SIZE=350|CAPTION= <scene name='initialview01'>1erz</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1erz", creates the "Structure Box" on the page.
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-carbamoyl-D-amino_acid_hydrolase N-carbamoyl-D-amino acid hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.77 3.5.1.77] </span>
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{{STRUCTURE_1erz| PDB=1erz | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1erz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1erz OCA], [http://www.ebi.ac.uk/pdbsum/1erz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1erz RCSB]</span>
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'''CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES'''
'''CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES'''
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[[Category: Yamamoto, M.]]
[[Category: Yamamoto, M.]]
[[Category: Yamashita, E.]]
[[Category: Yamashita, E.]]
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[[Category: four-layer sandwich]]
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[[Category: Four-layer sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:27:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:25 2008''
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Revision as of 12:27, 2 May 2008

Template:STRUCTURE 1erz

CRYSTAL STRUCTURE OF N-CARBAMYL-D-AMINO ACID AMIDOHYDROLASE WITH A NOVEL CATALYTIC FRAMEWORK COMMON TO AMIDOHYDROLASES


Overview

BACKGROUND: N-carbamyl-D-amino acid amidohydrolase (DCase) catalyzes the hydrolysis of N-carbamyl-D-amino acids to the corresponding D-amino acids, which are useful intermediates in the preparation of beta-lactam antibiotics. To understand the catalytic mechanism of N-carbamyl-D-amino acid hydrolysis, the substrate specificity and thermostability of the enzyme, we have determined the structure of DCase from Agrobacterium sp. strain KNK712. RESULTS: The crystal structure of DCase has been determined to 1.7 A resolution. The enzyme forms a homotetramer and each monomer consists of a variant of the alpha + beta fold. The topology of the enzyme comprises a sandwich of parallel beta sheets surrounded by two layers of alpha helices, this topology has not been observed in other amidohydrolases such as the N-terminal nucleophile (Ntn) hydrolases. CONCLUSIONS: The catalytic center could be identified and consists of Glu46, Lys126 and Cys171. Cys171 was found to be the catalytic nucleophile, and its nucleophilic character appeared to be increased through general-base activation by Glu46. DCase shows only weak sequence similarity with a family of amidohydrolases, including beta-alanine synthase, aliphatic amidases and nitrilases, but might share highly conserved residues in a novel framework, which could provide a possible explanation for the catalytic mechanism for this family of enzymes.

About this Structure

1ERZ is a Single protein structure of sequence from Agrobacterium sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases., Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T, Structure. 2000 Jul 15;8(7):729-37. PMID:10903946 Page seeded by OCA on Fri May 2 15:27:04 2008

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