1fo6
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=XE:XENON'>XE</scene> | |LIGAND= <scene name='pdbligand=XE:XENON'>XE</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Gamma-glutamyl_hydrolase Gamma-glutamyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.9 3.4.19.9] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Gamma-glutamyl_hydrolase Gamma-glutamyl hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.9 3.4.19.9] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo6 OCA], [http://www.ebi.ac.uk/pdbsum/1fo6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fo6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hsu, W H.]] | [[Category: Hsu, W H.]] | ||
[[Category: Wang, W C.]] | [[Category: Wang, W C.]] | ||
| - | [[Category: XE]] | ||
[[Category: four layer a/b fold]] | [[Category: four layer a/b fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:51 2008'' |
Revision as of 17:26, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Gamma-glutamyl hydrolase, with EC number 3.4.19.9 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE
Overview
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.
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
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