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==The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with MSMSMe==
==The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with MSMSMe==
<StructureSection load='4d4b' size='340' side='right' caption='[[4d4b]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
<StructureSection load='4d4b' size='340' side='right'caption='[[4d4b]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d4b]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D4B FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d4b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4B 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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MSX:1,6-DIDEOXY-DITHIO-METHYL-ALPHA-D-MANNOSE'>MSX</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]] 1.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d4a|4d4a]], [[4d4c|4d4c]], [[4d4d|4d4d]], [[5agd|5agd]]</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MSX:1,6-DIDEOXY-DITHIO-METHYL-ALPHA-D-MANNOSE'>MSX</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,6-alpha-mannosidase Mannan endo-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.101 3.2.1.101] </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=4d4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4b OCA], [https://pdbe.org/4d4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4b RCSB], [https://www.ebi.ac.uk/pdbsum/4d4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4b 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=4d4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4b OCA], [http://pdbe.org/4d4b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d4b RCSB], [http://www.ebi.ac.uk/pdbsum/4d4b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4b ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q9Z4P9_NIACI Q9Z4P9_NIACI]
alpha-Mannosidases and alpha-mannanases have attracted attention for the insight they provide into nucleophilic substitution at the hindered anomeric center of alpha-mannosides, and the potential of mannosidase inhibitors as cellular probes and therapeutic agents. We report the conformational itinerary of the family GH76 alpha-mannanases studied through structural analysis of the Michaelis complex and synthesis and evaluation of novel aza/imino sugar inhibitors. A Michaelis complex in an O S2 conformation, coupled with distortion of an azasugar in an inhibitor complex to a high energy B2,5 conformation are rationalized through ab initio QM/MM metadynamics that show how the enzyme surface restricts the conformational landscape of the substrate, rendering the B2,5 conformation the most energetically stable on-enzyme. We conclude that GH76 enzymes perform catalysis using an itinerary that passes through O S2 and B2,5 not equal conformations, information that should inspire the development of new antifungal agents.
 
Evidence for a Boat Conformation at the Transition State of GH76 alpha-1,6-Mannanases-Key Enzymes in Bacterial and Fungal Mannoprotein Metabolism.,Thompson AJ, Speciale G, Iglesias-Fernandez J, Hakki Z, Belz T, Cartmell A, Spears RJ, Chandler E, Temple MJ, Stepper J, Gilbert HJ, Rovira C, Williams SJ, Davies GJ Angew Chem Int Ed Engl. 2015 Mar 13. doi: 10.1002/anie.201410502. PMID:25772148<ref>PMID:25772148</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d4b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mannan endo-1,6-alpha-mannosidase]]
[[Category: Large Structures]]
[[Category: Belz, T]]
[[Category: Niallia circulans]]
[[Category: Cartmell, A]]
[[Category: Belz T]]
[[Category: Davies, G J]]
[[Category: Cartmell A]]
[[Category: Gilbert, H J]]
[[Category: Davies GJ]]
[[Category: Hakki, Z]]
[[Category: Gilbert HJ]]
[[Category: Iglesias-Fernandez, J]]
[[Category: Hakki Z]]
[[Category: Rovira, C]]
[[Category: Iglesias-Fernandez J]]
[[Category: Spears, R J]]
[[Category: Rovira C]]
[[Category: Speciale, G]]
[[Category: Spears RJ]]
[[Category: Stepper, J]]
[[Category: Speciale G]]
[[Category: Thompson, A J]]
[[Category: Stepper J]]
[[Category: Williams, S J]]
[[Category: Thompson AJ]]
[[Category: Cazy]]
[[Category: Williams SJ]]
[[Category: Enzyme-carbohydrate interaction]]
[[Category: Gh76]]
[[Category: Glycosidase inhibition]]
[[Category: Glycoside hydrolase]]
[[Category: Hydrolase]]
[[Category: Mannan]]
[[Category: Quantum mechanic]]
[[Category: Transition state]]

Latest revision as of 07:19, 1 May 2024

The catalytic domain, BcGH76, of Bacillus circulans Aman6 in complex with MSMSMe

4d4b, resolution 1.30Å

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