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| | <StructureSection load='4c1o' size='340' side='right'caption='[[4c1o]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4c1o' size='340' side='right'caption='[[4c1o]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c1o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"parageobacillus_thermoglucosidasius"_(suzuki_et_al._1984)_aliyu_et_al._2016 "parageobacillus thermoglucosidasius" (suzuki et al. 1984) aliyu et al. 2016]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C1O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c1o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parageobacillus_thermoglucosidasius Parageobacillus thermoglucosidasius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C1O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c1p|4c1p]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylan_1,4-beta-xylosidase Xylan 1,4-beta-xylosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.37 3.2.1.37] </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=4c1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1o OCA], [https://pdbe.org/4c1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c1o RCSB], [https://www.ebi.ac.uk/pdbsum/4c1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1o ProSAT]</span></td></tr> |
| - | <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=4c1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c1o OCA], [http://pdbe.org/4c1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c1o RCSB], [http://www.ebi.ac.uk/pdbsum/4c1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c1o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A067XG64_PARTM A0A067XG64_PARTM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Xylosidase|Xylosidase]] | + | *[[Xylosidase 3D structures|Xylosidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Xylan 1,4-beta-xylosidase]] | + | [[Category: Parageobacillus thermoglucosidasius]] |
| - | [[Category: Crennell, S J]] | + | [[Category: Crennell SJ]] |
| - | [[Category: Danson, M J]] | + | [[Category: Danson MJ]] |
| - | [[Category: Eley, K]] | + | [[Category: Eley K]] |
| - | [[Category: Espina, G]] | + | [[Category: Espina G]] |
| - | [[Category: Schneider, T R]] | + | [[Category: Schneider TR]] |
| - | [[Category: Gh52]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
4c1o is a 1 chain structure with sequence from Parageobacillus thermoglucosidasius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.7Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A0A067XG64_PARTM
Publication Abstract from PubMed
Geobacillus thermoglucosidasius is a thermophilic bacterium that is able to ferment both C6 and C5 sugars to produce ethanol. During growth on hemicellulose biomass, an intracellular beta-xylosidase catalyses the hydrolysis of xylo-oligosaccharides to the monosaccharide xylose, which can then enter the pathways of central metabolism. The gene encoding a G. thermoglucosidasius beta-xylosidase belonging to CAZy glycoside hydrolase family GH52 has been cloned and expressed in Escherichia coli. The recombinant enzyme has been characterized and a high-resolution (1.7 A) crystal structure has been determined, resulting in the first reported structure of a GH52 family member. A lower resolution (2.6 A) structure of the enzyme-substrate complex shows the positioning of the xylobiose substrate to be consistent with the proposed retaining mechanism of the family; additionally, the deep cleft of the active-site pocket, plus the proximity of the neighbouring subunit, afford an explanation for the lack of catalytic activity towards the polymer xylan. Whilst the fold of the G. thermoglucosidasius beta-xylosidase is completely different from xylosidases in other CAZy families, the enzyme surprisingly shares structural similarities with other glycoside hydrolases, despite having no more than 13% sequence identity.
A novel beta-xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds.,Espina G, Eley K, Pompidor G, Schneider TR, Crennell SJ, Danson MJ Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1366-74. doi:, 10.1107/S1399004714002788. Epub 2014 Apr 30. PMID:24816105[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Espina G, Eley K, Pompidor G, Schneider TR, Crennell SJ, Danson MJ. A novel beta-xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1366-74. doi:, 10.1107/S1399004714002788. Epub 2014 Apr 30. PMID:24816105 doi:http://dx.doi.org/10.1107/S1399004714002788
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