1fo6
From Proteopedia
(New page: 200px<br /><applet load="1fo6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fo6, resolution 1.95Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1fo6.jpg|left|200px]]<br /><applet load="1fo6" size=" | + | [[Image:1fo6.jpg|left|200px]]<br /><applet load="1fo6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fo6, resolution 1.95Å" /> | caption="1fo6, resolution 1.95Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The N-carbamoyl-D-amino-acid amidohydrolase (D-NCAase) is used on an | + | 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== | ==About this Structure== | ||
| - | 1FO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with XE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1FO6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gamma-glutamyl hydrolase]] | [[Category: Gamma-glutamyl hydrolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chen, C | + | [[Category: Chen, C Y.]] |
| - | [[Category: Chien, F | + | [[Category: Chien, F T.]] |
| - | [[Category: Hsu, W | + | [[Category: Hsu, W H.]] |
| - | [[Category: Wang, W | + | [[Category: Wang, W C.]] |
[[Category: XE]] | [[Category: XE]] | ||
[[Category: four layer a/b fold]] | [[Category: four layer a/b fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:46 2008'' |
Revision as of 10:40, 21 February 2008
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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 with as ligand. Active as Gamma-glutamyl hydrolase, with EC number 3.4.19.9 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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