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{{STRUCTURE_4cd7|  PDB=4cd7  |  SCENE=  }}
==The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose==
===The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose===
<StructureSection load='4cd7' size='340' side='right' caption='[[4cd7]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
{{ABSTRACT_PUBMED_24339341}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4cd7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CD7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IFM:5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE'>IFM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cd4|4cd4]], [[4cd5|4cd5]], [[4cd6|4cd6]], [[4cd8|4cd8]]</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-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </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=4cd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4cd7 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mannosidases catalyze the hydrolysis of a diverse range of polysaccharides and glycoconjugates, and the various sequence-based mannosidase families have evolved ingenious strategies to overcome the stereoelectronic challenges of mannoside chemistry. Using a combination of computational chemistry, inhibitor design and synthesis, and X-ray crystallography of inhibitor/enzyme complexes, it is demonstrated that mannoimidazole-type inhibitors are energetically poised to report faithfully on mannosidase transition-state conformation, and provide direct evidence for the conformational itinerary used by diverse mannosidases, including beta-mannanases from families GH26 and GH113. Isofagomine-type inhibitors are poor mimics of transition-state conformation, owing to the high energy barriers that must be crossed to attain mechanistically relevant conformations, however, these sugar-shaped heterocycles allow the acquisition of ternary complexes that span the active site, thus providing valuable insight into active-site residues involved in substrate recognition.


==About this Structure==
Combined inhibitor free-energy landscape and structural analysis reports on the mannosidase conformational coordinate.,Williams RJ, Iglesias-Fernandez J, Stepper J, Jackson A, Thompson AJ, Lowe EC, White JM, Gilbert HJ, Rovira C, Davies GJ, Williams SJ Angew Chem Int Ed Engl. 2014 Jan 20;53(4):1087-91. doi: 10.1002/anie.201308334., Epub 2013 Dec 11. PMID:24339341<ref>PMID:24339341</ref>
[[4cd7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<ref group="xtra">PMID:024339341</ref><references group="xtra"/><references/>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 27009]]
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Davies, G J.]]
[[Category: Davies, G J]]
[[Category: Gilbert, H J.]]
[[Category: Gilbert, H J]]
[[Category: Iglesias-Fernandez, J.]]
[[Category: Iglesias-Fernandez, J]]
[[Category: Jackson, A.]]
[[Category: Jackson, A]]
[[Category: Lowe, E C.]]
[[Category: Lowe, E C]]
[[Category: Rovira, C.]]
[[Category: Rovira, C]]
[[Category: Stepper, J.]]
[[Category: Stepper, J]]
[[Category: Thompson, A J.]]
[[Category: Thompson, A J]]
[[Category: White, J M.]]
[[Category: White, J M]]
[[Category: Williams, R J.]]
[[Category: Williams, R J]]
[[Category: Williams, S J.]]
[[Category: Williams, S J]]
[[Category: Beta-mannosidase]]
[[Category: Beta-mannosidase]]
[[Category: Biocatalysis]]
[[Category: Biocatalysis]]

Revision as of 14:19, 4 January 2015

The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose

4cd7, resolution 1.65Å

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