5m0x: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 5m0x is ON HOLD
+==Structure of apo structure of GH36 alpha-galactosidase from Thermotoga maritima==
+<StructureSection load='5m0x' size='340' side='right'caption='[[5m0x]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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='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>
+</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;">
+== 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.
-Authors: Pengelly, R., Gloster, T.
+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<ref>PMID:27783466</ref>
-Description: Structure of apo structure of GH36 alpha-galactosidase from Thermotoga maritima
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Pengelly, R]]
+<div class="pdbe-citations 5m0x" style="background-color:#fffaf0;"></div>
-[[Category: Gloster, T]]
+==See Also==
+*[[Galactosidase 3D structures|Galactosidase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Thermotoga maritima]]
+[[Category: Gloster T]]
+[[Category: Pengelly R]]