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3vay

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Current revision (08:39, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3vay' size='340' side='right'caption='[[3vay]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
<StructureSection load='3vay' size='340' side='right'caption='[[3vay]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vay]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Psesm Psesm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VAY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vay]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato_str._DC3000 Pseudomonas syringae pv. tomato str. DC3000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VAY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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]] 1.979&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSPTO_0221 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223283 PSESM])</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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3vay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vay OCA], [https://pdbe.org/3vay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vay RCSB], [https://www.ebi.ac.uk/pdbsum/3vay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vay ProSAT]</span></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=3vay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vay OCA], [https://pdbe.org/3vay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vay RCSB], [https://www.ebi.ac.uk/pdbsum/3vay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vay ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q88B12_PSESM Q88B12_PSESM]
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2-Haloacid dehalogenases (2-HADs) catalyse the hydrolytic dehalogenation of 2-haloalkanoic acids, cleaving the carbon-halide bond at the C(alpha)-atom position and releasing a halogen atom. These enzymes are of interest for their potential use in bioremediation and in the synthesis of industrial chemicals. Here, the crystal structure of 2-HAD from Pseudomonas syringae pv. tomato DC3000 (ps-2-HAD) at 1.98 A resolution solved using the single-wavelength anomalous dispersion method is reported. The ps-2-HAD molecule consists of two structurally distinct domains: the core domain and the subdomain. Enzymatic activity analysis of ps-2-HAD revealed its capacity to catalyse the dehalogenation of both L- and D-substrates; however, the structure of ps-2-HAD is completely different from that of DehI, which is the only DL-2-HAD enzyme that has been structurally characterized, but shows similar overall folding to L-HADs. Single mutations of four amino-acid residues at the putative active site showed that they are related to its enzymatic activity, yet three of them are nonconserved among HADs. These observations imply that ps-2-HAD has a novel active site and a unique catalytic behaviour compared with other HADs. This study provides a structural basis and biochemical evidence for further elucidation of the catalytic mechanism of 2-HAD.
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Structure of 2-haloacid dehalogenase from Pseudomonas syringae pv. tomato DC3000.,Hou Z, Zhang H, Li M, Chang W Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1108-14. doi:, 10.1107/S0907444913006021. Epub 2013 May 15. PMID:23695255<ref>PMID:23695255</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vay" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Psesm]]
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[[Category: Pseudomonas syringae pv. tomato str. DC3000]]
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[[Category: Chang, W]]
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[[Category: Chang W]]
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[[Category: Hou, Z]]
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[[Category: Hou Z]]
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[[Category: Li, M]]
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[[Category: Li M]]
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[[Category: Zhang, H]]
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[[Category: Zhang H]]
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[[Category: Haloacid dehalogenase]]
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[[Category: Hydrolase]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of 2-Haloacid Dehalogenase from Pseudomonas syringae pv. Tomato DC3000

PDB ID 3vay

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