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| | <StructureSection load='7c7d' size='340' side='right'caption='[[7c7d]], [[Resolution|resolution]] 1.16Å' scene=''> | | <StructureSection load='7c7d' size='340' side='right'caption='[[7c7d]], [[Resolution|resolution]] 1.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7c7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_thermodiastaticus"_bergey_et_al._1923 "actinomyces thermodiastaticus" bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C7D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C7D FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C7D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.59 3.2.1.59] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7d OCA], [http://pdbe.org/7c7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c7d RCSB], [http://www.ebi.ac.uk/pdbsum/7c7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7d 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=7c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c7d OCA], [https://pdbe.org/7c7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c7d RCSB], [https://www.ebi.ac.uk/pdbsum/7c7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c7d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces thermodiastaticus bergey et al. 1923]] | |
| - | [[Category: Hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hayashi, J]] | + | [[Category: Hayashi J]] |
| - | [[Category: Hibi, T]] | + | [[Category: Hibi T]] |
| - | [[Category: Itoh, T]] | + | [[Category: Itoh T]] |
| - | [[Category: Panti, N]] | + | [[Category: Panti N]] |
| - | [[Category: Suyotha, W]] | + | [[Category: Suyotha W]] |
| - | [[Category: Toyotake, Y]] | + | [[Category: Toyotake Y]] |
| - | [[Category: Wakayama, M]] | + | [[Category: Wakayama M]] |
| - | [[Category: Yano, S]] | + | [[Category: Yano S]] |
| - | [[Category: Glycosidase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
alpha-1,3-Glucan is a homopolymer composed of D-glucose (Glc) and it is an extracellular polysaccharide found in dental plaque due to Streptococcus species. alpha-1,3-Glucanase from Streptomyces thermodiastaticus strain HF3-3 (Agl-ST) has been identified as a thermostable alpha-1,3-glucanase, which is classified into glycoside hydrolase family 87 (GH87) and specifically hydrolyzes alpha-1,3-glucan with an endo-action. The enzyme has a potential to inhibit the production of dental plaque and to be used for biotechnological applications. Here we show the structure of the catalytic unit of Agl-ST determined at 1.16 A resolution using X-ray crystallography. The catalytic unit is composed of two modules, a beta-sandwich fold module, and a right-handed beta-helix fold module, which resembles other structural characterized GH87 enzymes from Bacillus circulans str. KA-304 and Paenibacillus glycanilyticus str. FH11, with moderate sequence identities between each other (approximately 27% between the catalytic units). However, Agl-ST is smaller in size and more thermally stable than the others. A disulfide bond that anchors the C-terminal coil of the beta-helix fold, which is expected to contribute to thermal stability only exists in the catalytic unit of Agl-ST.
Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3.,Itoh T, Panti N, Hayashi J, Toyotake Y, Matsui D, Yano S, Wakayama M, Hibi T Biochem Biophys Res Commun. 2020 Oct 8. pii: S0006-291X(20)31894-5. doi:, 10.1016/j.bbrc.2020.09.133. PMID:33041007[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Itoh T, Panti N, Hayashi J, Toyotake Y, Matsui D, Yano S, Wakayama M, Hibi T. Crystal structure of the catalytic unit of thermostable GH87 alpha-1,3-glucanase from Streptomyces thermodiastaticus strain HF3-3. Biochem Biophys Res Commun. 2020 Oct 8. pii: S0006-291X(20)31894-5. doi:, 10.1016/j.bbrc.2020.09.133. PMID:33041007 doi:http://dx.doi.org/10.1016/j.bbrc.2020.09.133
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