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New page: left|200px<br /><applet load="1nba" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nba, resolution 2.0Å" /> '''CRYSTAL STRUCTURE ANA...
 
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[[Image:1nba.gif|left|200px]]<br /><applet load="1nba" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nba, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION==
N-carbamoylsarcosine amidohydrolase from Arthrobacter sp., a tetramer of, polypeptides with 264 amino acid residues each, has been crystallized and, its structure solved and refined at 2.0 A resolution, to a, crystallographic R-factor of 18.6%. The crystals employed in the analysis, contain one tetramer of 116,000 M(r) in the asymmetric unit. The structure, determination proceeded by multiple isomorphous replacement, followed by, solvent-flattening and density averaging about the local diads within the, tetramer. In the final refined model, the root-mean-square deviation from, ideality is 0.01 A for bond distances and 2.7 degrees for bond angles. The, asymmetric unit consists of 7853 protein atoms, 431 water molecules and, four sulfate ions bound into the putative active site clefts in each, subunit. One subunit contains a central six-stranded parallel beta-pleated, sheet packed by helices on both sides. On one side, two helices face the, solvent, while two of the helices on the other side are buried in the, tight intersubunit contacts. The catalytic center of the enzyme, tentatively identified by inhibitor binding, is located at the interface, between two subunits and involves residues from both. It is suggested that, the nucleophilic group involved in hydrolysis of the substrate is the, thiol group of Cys117 and a nucleophilic addition-elimination mechanism is, proposed.
<StructureSection load='1nba' size='340' side='right'caption='[[1nba]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1nba]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBA FirstGlance]. <br>
1NBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/N-carbamoylsarcosine_amidase N-carbamoylsarcosine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.59 3.5.1.59] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NBA OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nba OCA], [https://pdbe.org/1nba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nba RCSB], [https://www.ebi.ac.uk/pdbsum/1nba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nba ProSAT]</span></td></tr>
Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution., Romao MJ, Turk D, Gomis-Ruth FX, Huber R, Schumacher G, Mollering H, Russmann L, J Mol Biol. 1992 Aug 20;226(4):1111-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1381445 1381445]
</table>
[[Category: Arthrobacter sp.]]
== Function ==
[[Category: N-carbamoylsarcosine amidase]]
[https://www.uniprot.org/uniprot/CSH_ARTSP CSH_ARTSP]
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Gomis-Ruth, F.Z.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Huber, R.]]
Check<jmol>
[[Category: Mollering, H.]]
  <jmolCheckbox>
[[Category: Romao, M.J.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/1nba_consurf.spt"</scriptWhenChecked>
[[Category: Russmann, L.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Schumacher, G.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Turk, D.]]
  </jmolCheckbox>
[[Category: SO4]]
</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=1nba ConSurf].
[[Category: hydrolase(in linear amides)]]
<div style="clear:both"></div>
 
__TOC__
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:06:46 2007''
</StructureSection>
[[Category: Arthrobacter sp]]
[[Category: Large Structures]]
[[Category: Gomis-Ruth F-Z]]
[[Category: Huber R]]
[[Category: Mollering H]]
[[Category: Romao MJ]]
[[Category: Russmann L]]
[[Category: Schumacher G]]
[[Category: Turk D]]

Latest revision as of 07:54, 14 February 2024

CRYSTAL STRUCTURE ANALYSIS, REFINEMENT AND ENZYMATIC REACTION MECHANISM OF N-CARBAMOYLSARCOSINE AMIDOHYDROLASE FROM ARTHROBACTER SP. AT 2.0 ANGSTROMS RESOLUTION

1nba, resolution 2.00Å

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