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1din

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(New page: 200px<br /><applet load="1din" size="450" color="white" frame="true" align="right" spinBox="true" caption="1din, resolution 1.8&Aring;" /> '''DIENELACTONE HYDROLAS...)
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[[Image:1din.jpg|left|200px]]<br /><applet load="1din" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1din, resolution 1.8&Aring;" />
 
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'''DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS'''<br />
 
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==Overview==
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==DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS==
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The structure of dienelactone hydrolase (DLH) from Pseudomonus sp. B13, after stereochemically restrained least-squares refinement at 1.8 A, resolution, is described. The final molecular model of DLH has a, conventional R value of 0.150 and includes all but the carboxyl-terminal, three residues that are crystallographically disordered. The positions of, 279 water molecules are included in the final model. The root-mean-square, deviation from ideal bond distances for the model is 0.014 A and the error, in atomic co-ordinates is estimated to be 0.15 A. DLH is a monomeric, enzyme containing 236 amino acid residues and is a member of the, beta-ketoadipate pathway found in bacteria and fungi. DLH is an alpha/beta, protein containing seven helices and eight strands of beta-pleated sheet., A single 4-turn 3(10)-helix is seen. The active-site Cys123 residues at, the N-terminal end of an alpha-helix that is peculiar in its consisting, entirely of hydrophobic residues (except for a C-terminal lysine). The, beta-sheet is composed of parallel strands except for strand 2, which, gives rise to a short antiparallel region at the N-terminal end of the, central beta-sheet. The active-site cysteine residue is part of a triad of, residues consisting of Cys123, His202 and Asp171, and is reminiscent of, the serine/cysteine proteases. As in papain and actinidin, the active, thiol is partially oxidized during X-ray data collection. The positions of, both the reduced and the oxidized sulphur are described. The active site, geometry suggests that a change in the conformation of the native thiol, occurs upon diffusion of substrate into the active site cleft of DLH. This, enables nucleophilic attack by the gamma-sulphur to occur on the cyclic, ester substrate through a ring-opening reaction.
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<StructureSection load='1din' size='340' side='right'caption='[[1din]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1din]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_knackmussii Pseudomonas knackmussii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DIN FirstGlance]. <br>
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1DIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Active as [http://en.wikipedia.org/wiki/Carboxymethylenebutenolidase Carboxymethylenebutenolidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.45 3.1.1.45] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DIN 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]] 1.8&#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=CSD:3-SULFINOALANINE'>CSD</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=1din FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1din OCA], [https://pdbe.org/1din PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1din RCSB], [https://www.ebi.ac.uk/pdbsum/1din PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1din ProSAT]</span></td></tr>
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Refined structure of dienelactone hydrolase at 1.8 A., Pathak D, Ollis D, J Mol Biol. 1990 Jul 20;214(2):497-525. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2380986 2380986]
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</table>
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[[Category: Carboxymethylenebutenolidase]]
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== Function ==
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[[Category: Pseudomonas sp.]]
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[https://www.uniprot.org/uniprot/CLCD_PSEKB CLCD_PSEKB] Ring cleavage of cyclic ester dienelactone to produce maleylacetate.
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Ollis, D.L.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Pathak, D.]]
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Check<jmol>
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[[Category: aromatic hydrocarbon catabolism]]
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<jmolCheckbox>
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[[Category: carboxymethylenebutenolidase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1din_consurf.spt"</scriptWhenChecked>
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[[Category: dienelactone hydrolase]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: hydrolytic enzyme]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: serine esterase]]
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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=1din ConSurf].
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:18:23 2007''
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas knackmussii]]
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[[Category: Ollis DL]]
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[[Category: Pathak D]]

Current revision

DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS

PDB ID 1din

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