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| | <StructureSection load='5m0x' size='340' side='right'caption='[[5m0x]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5m0x' size='340' side='right'caption='[[5m0x]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m0x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M0X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M0X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M0X FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">galA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </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=5m0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m0x OCA], [https://pdbe.org/5m0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m0x RCSB], [https://www.ebi.ac.uk/pdbsum/5m0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m0x ProSAT]</span></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=5m0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m0x OCA], [http://pdbe.org/5m0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m0x RCSB], [http://www.ebi.ac.uk/pdbsum/5m0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m0x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AGAL_THEMA AGAL_THEMA] Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.<ref>PMID:25486100</ref> <ref>PMID:9741105</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-galactosidase]] | |
| - | [[Category: Atcc 43589]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gloster, T]] | + | [[Category: Thermotoga maritima]] |
| - | [[Category: Pengelly, R]] | + | [[Category: Gloster T]] |
| - | [[Category: Glycoside hydrolase]] | + | [[Category: Pengelly R]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
AGAL_THEMA Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.[1] [2]
Publication Abstract from PubMed
Glycoside hydrolases (GHs) have attracted considerable attention as targets for therapeutic agents, and thus mechanism-based inhibitors are of great interest. We report the first structural analysis of a carbocyclic mechanism-based GH inactivator, the results of which show that the two Michaelis complexes are in 2 H3 conformations. We also report the synthesis and reactivity of a fluorinated analogue and the structure of its covalently linked intermediate (flattened 2 H3 half-chair). We conclude that these inactivator reactions mainly involve motion of the pseudo-anomeric carbon atom, knowledge that should stimulate the design of new transition-state analogues for use as chemical biology tools.
Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars.,Adamson C, Pengelly RJ, Shamsi Kazem Abadi S, Chakladar S, Draper J, Britton R, Gloster TM, Bennet AJ Angew Chem Int Ed Engl. 2016 Nov 21;55(48):14978-14982. doi:, 10.1002/anie.201607431. Epub 2016 Oct 26. PMID:27783466[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Borisova AS, Ivanen DR, Bobrov KS, Eneyskaya EV, Rychkov GN, Sandgren M, Kulminskaya AA, Sinnott ML, Shabalin KA. alpha-Galactobiosyl units: thermodynamics and kinetics of their formation by transglycosylations catalysed by the GH36 alpha-galactosidase from Thermotoga maritima. Carbohydr Res. 2015 Jan 12;401:115-21. doi: 10.1016/j.carres.2014.11.003. Epub, 2014 Nov 21. PMID:25486100 doi:http://dx.doi.org/10.1016/j.carres.2014.11.003
- ↑ Liebl W, Wagner B, Schellhase J. Properties of an alpha-galactosidase, and structure of its gene galA, within an alpha-and beta-galactoside utilization gene cluster of the hyperthermophilic bacterium Thermotoga maritima. Syst Appl Microbiol. 1998 Mar;21(1):1-11. PMID:9741105
- ↑ Adamson C, Pengelly RJ, Shamsi Kazem Abadi S, Chakladar S, Draper J, Britton R, Gloster TM, Bennet AJ. Structural Snapshots for Mechanism-Based Inactivation of a Glycoside Hydrolase by Cyclopropyl Carbasugars. Angew Chem Int Ed Engl. 2016 Nov 21;55(48):14978-14982. doi:, 10.1002/anie.201607431. Epub 2016 Oct 26. PMID:27783466 doi:http://dx.doi.org/10.1002/anie.201607431
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