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[[Image:1fo6.jpg|left|200px]]


{{Structure
==CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE==
|PDB= 1fo6 |SIZE=350|CAPTION= <scene name='initialview01'>1fo6</scene>, resolution 1.95&Aring;
<StructureSection load='1fo6' size='340' side='right'caption='[[1fo6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=XE:XENON'>XE</scene>
<table><tr><td colspan='2'>[[1fo6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FO6 FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo6 OCA], [https://pdbe.org/1fo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo6 ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE'''
== Function ==
 
[https://www.uniprot.org/uniprot/DCAS_RHIRD DCAS_RHIRD] The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fo6_consurf.spt"</scriptWhenChecked>
1FO6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO6 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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:[http://www.ncbi.nlm.nih.gov/pubmed/11237598 11237598]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fo6 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Gamma-glutamyl hydrolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Chen C-Y]]
[[Category: Chen, C Y.]]
[[Category: Chien F-T]]
[[Category: Chien, F T.]]
[[Category: Hsu W-H]]
[[Category: Hsu, W H.]]
[[Category: Wang W-C]]
[[Category: Wang, W C.]]
[[Category: XE]]
[[Category: four layer a/b fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:48 2008''
Retrieved from "https://proteopedia.org/1fo6"