4wvc

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<StructureSection load='4wvc' size='340' side='right'caption='[[4wvc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4wvc' size='340' side='right'caption='[[4wvc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4wvc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WVC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4wvc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WVC 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z07|2z07]], [[4wva|4wva]], [[4wvb|4wvb]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TTHA0978 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=4wvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvc OCA], [https://pdbe.org/4wvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wvc RCSB], [https://www.ebi.ac.uk/pdbsum/4wvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvc ProSAT]</span></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=4wvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wvc OCA], [http://pdbe.org/4wvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wvc RCSB], [http://www.ebi.ac.uk/pdbsum/4wvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wvc ProSAT]</span></td></tr>
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</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/Q5SJN0_THET8 Q5SJN0_THET8]
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Glycoside hydrolase family 63 (GH63) proteins are found in eukaryotes such as processing alpha-glucosidase I and also many bacteria and archaea. Recent studies have identified two bacterial and one plant GH63 mannosylglycerate hydrolases that act on both glucosylglycerate and mannosylglycerate, which are compatible solutes found in many thermophilic prokaryotes and some plants. Here we report the 1.67-A crystal structure of one of these GH63 mannosylglycerate hydrolases, Tt8MGH from Thermus thermophilus HB8, which is 99% homologous to mannosylglycerate hydrolase from T.thermophilus HB27. Tt8MGH consists of a single (alpha/alpha)6-barrel catalytic domain with two additional helices and two long loops which form a homotrimer. The structures of this protein in complexes with glucose or glycerate were also determined at 1.77- or 2.10-A resolution, respectively. A comparison of these structures revealed that the conformations of three flexible loops were largely different from each other. The conformational changes may be induced by ligand binding and serve to form finger-like structures for holding substrates. These findings represent the first-ever proposed substrate recognition mechanism for GH63 mannosylglycerate hydrolase.
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Crystal structure and substrate-binding mode of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8.,Miyazaki T, Ichikawa M, Iino H, Nishikawa A, Tonozuka T J Struct Biol. 2015 Feb 21. pii: S1047-8477(15)00037-4. doi:, 10.1016/j.jsb.2015.02.006. PMID:25712767<ref>PMID:25712767</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 4wvc" 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: Thet8]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Ichikawa, M]]
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[[Category: Ichikawa M]]
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[[Category: Miyazaki, T]]
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[[Category: Miyazaki T]]
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[[Category: Nishikawa, A]]
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[[Category: Nishikawa A]]
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[[Category: Tonozuka, T]]
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[[Category: Tonozuka T]]
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[[Category: Gh63]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of GH63 mannosylglycerate hydrolase from Thermus thermophilus HB8 in complex with Tris and D-glycerate

PDB ID 4wvc

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