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4ygq

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==Crystal structure of HAD phosphatase from Thermococcus onnurineus==
==Crystal structure of HAD phosphatase from Thermococcus onnurineus==
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<StructureSection load='4ygq' size='340' side='right' caption='[[4ygq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4ygq' size='340' side='right'caption='[[4ygq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ygq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YGQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ygq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_onnurineus_NA1 Thermococcus onnurineus NA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YGQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</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]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ygs|4ygs]], [[4ygr|4ygr]]</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=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ygq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ygq OCA], [http://pdbe.org/4ygq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ygq RCSB], [http://www.ebi.ac.uk/pdbsum/4ygq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ygq ProSAT]</span></td></tr>
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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=4ygq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ygq OCA], [https://pdbe.org/4ygq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ygq RCSB], [https://www.ebi.ac.uk/pdbsum/4ygq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ygq 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/B6YTD6_THEON B6YTD6_THEON]
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Proteins in the haloalkaloic acid dehalogenase (HAD) superfamily, which is one of the largest enzyme families, is generally composed of a catalytic core domain and a cap domain. Although proteins in this family show broad substrate specificities, the mechanisms of their substrate recognition are not well understood. In this study, we identified a new substrate binding motif of HAD proteins from structural and functional analyses, and propose that this motif might be crucial for interacting with hydrophobic rings of substrates. The crystal structure of TON_0338, one of the 17 putative HAD proteins identified in a hyperthermophilic archaeon, Thermococcus onnurineus NA1, was determined as an apo-form at 2.0 A resolution. In addition, we determined the crystal structure TON_0338 in complex with Mg2+ or N-cyclohexyl-2-aminoethanesulfonic acid (CHES) at 1.7 A resolution. Examination of the apo-form and CHES-bound structures revealed that CHES is sandwiched between Trp58 and Trp61, suggesting that this Trp sandwich might function as a substrate recognition motif. In the phosphatase assay, TON_0338 was shown to have high activity for flavin mononucleotide (FMN), and the docking analysis suggested that the flavin of FMN may interact with Trp58 and Trp61 in a way similar to that observed in the crystal structure. Moreover, the replacement of these tryptophan residues significantly reduced the phosphatase activity for FMN. Our results suggest that WxxW may function as a substrate binding motif in HAD proteins, and expand the diversity of their substrate recognition mode.
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Structural basis for the substrate selectivity of a HAD phosphatase from Thermococcus onnurineus NA1.,Ngo TD, Van Le B, Subramani VK, Thi Nguyen CM, Lee HS, Cho Y, Kim KK, Hwang HY Biochem Biophys Res Commun. 2015 Apr 6. pii: S0006-291X(15)00647-6. doi:, 10.1016/j.bbrc.2015.03.179. PMID:25858319<ref>PMID:25858319</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 4ygq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cho, Y]]
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[[Category: Large Structures]]
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[[Category: Hwang, H Y]]
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[[Category: Thermococcus onnurineus NA1]]
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[[Category: Kim, K K]]
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[[Category: Cho Y]]
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[[Category: Le, B V]]
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[[Category: Hwang HY]]
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[[Category: Lee, H S]]
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[[Category: Kim KK]]
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[[Category: Ngo, T D]]
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[[Category: Le BV]]
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[[Category: Nguyen, C M.T]]
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[[Category: Lee HS]]
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[[Category: Subramani, V K]]
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[[Category: Ngo TD]]
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[[Category: Had phosphatase]]
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[[Category: Nguyen CMT]]
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[[Category: Hydrolase]]
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[[Category: Subramani VK]]
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[[Category: Substrate selectivity]]
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Current revision

Crystal structure of HAD phosphatase from Thermococcus onnurineus

PDB ID 4ygq

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