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5m0x

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Structure of apo structure of GH36 alpha-galactosidase from Thermotoga maritima

Structural highlights

5m0x is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5m0x"

Categories: Large Structures | Thermotoga maritima | Gloster T | Pengelly R

@@ Line 1: / Line 1: @@
-'''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]]

5m0x

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Current revision

Structure of apo structure of GH36 alpha-galactosidase from Thermotoga maritima

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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