View source for 4cd8


==The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManMIm==
<StructureSection load='4cd8' size='340' side='right'caption='[[4cd8]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CD8 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]] 1.47&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MVL:(5R,6R,7S,8R)-5-(HYDROXYMETHYL)-5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>MVL</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=4cd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd8 OCA], [https://pdbe.org/4cd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cd8 RCSB], [https://www.ebi.ac.uk/pdbsum/4cd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A5H1I6_9BACL A5H1I6_9BACL] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cd8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alicyclobacillus acidocaldarius]]
[[Category: Large Structures]]
[[Category: Davies GJ]]
[[Category: Gilbert HJ]]
[[Category: Iglesias-Fernandez J]]
[[Category: Jackson A]]
[[Category: Lowe EC]]
[[Category: Rovira C]]
[[Category: Stepper J]]
[[Category: Thompson AJ]]
[[Category: White JM]]
[[Category: Williams RJ]]
[[Category: Williams SJ]]