1fo6

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(New page: 200px<br /><applet load="1fo6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fo6, resolution 1.95&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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[[Image:1fo6.jpg|left|200px]]<br /><applet load="1fo6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fo6, resolution 1.95&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF N-CARBAMoYL-D-AMINO-ACID AMIDOHYDROLASE==
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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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<StructureSection load='1fo6' size='340' side='right'caption='[[1fo6]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FO6 OCA].
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</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>
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<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>
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==Reference==
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<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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11237598 11237598]
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fo6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
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[[Category: Gamma-glutamyl hydrolase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen C-Y]]
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[[Category: Chen, C.Y.]]
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[[Category: Chien F-T]]
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[[Category: Chien, F.T.]]
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[[Category: Hsu W-H]]
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[[Category: Hsu, W.H.]]
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[[Category: Wang W-C]]
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[[Category: Wang, W.C.]]
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[[Category: XE]]
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[[Category: four layer a/b fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:05:10 2007''
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Current revision

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

PDB ID 1fo6

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