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1fo6

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{{STRUCTURE_1fo6| PDB=1fo6 | SCENE= }}
{{STRUCTURE_1fo6| PDB=1fo6 | SCENE= }}
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'''CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE'''
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===CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE===
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==Overview==
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The N-carbamoyl-D-amino-acid amidohydrolase (D-NCAase) is used on an industrial scale for the production of D-amino acids. The crystal structure of D-NCAase was solved by multiple isomorphous replacement with anomalous scattering using xenon and gold derivatives, and refined to 1.95 A resolution, to an R-factor of 18.6 %. The crystal structure shows a four-layer alpha/beta fold with two six-stranded beta sheets packed on either side by two alpha helices. One exterior layer faces the solvent, whereas the other one is buried and involved in the tight intersubunit contacts. A long C-terminal fragment extends from a monomer to a site near a dyad axis, and associates with another monomer to form a small and hydrophobic cavity, where a xenon atom can bind. Site-directed mutagenesis of His129, His144 and His215 revealed strict geometric requirements of these conserved residues to maintain a stable conformation of a putative catalytic cleft. A region located within this cleft involving Cys172, Glu47, and Lys127 is proposed for D-NCAase catalysis and is similar to the Cys-Asp-Lys site of N-carbamoylsarcosine amidohydrolase. The homologous active-site framework of these enzymes with distinct structures suggests convergent evolution of a common catalytic mechanism.
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{{ABSTRACT_PUBMED_11237598}}
==About this Structure==
==About this Structure==
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[[Category: Wang, W C.]]
[[Category: Wang, W C.]]
[[Category: Four layer a/b fold]]
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Revision as of 00:40, 1 July 2008

Image:1fo6.png

Template:STRUCTURE 1fo6

CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE

Template:ABSTRACT PUBMED 11237598

About this Structure

1FO6 is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft., Wang WC, Hsu WH, Chien FT, Chen CY, J Mol Biol. 2001 Feb 16;306(2):251-61. PMID:11237598

Page seeded by OCA on Tue Jul 1 03:40:01 2008

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