View source for 4ayo


==Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31==
<StructureSection load='4ayo' size='340' side='right'caption='[[4ayo]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ayo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_sp._K31 Caulobacter sp. K31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYO 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]] 0.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4ayo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayo OCA], [https://pdbe.org/4ayo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayo RCSB], [https://www.ebi.ac.uk/pdbsum/4ayo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B0SWV2_CAUSK B0SWV2_CAUSK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mannosides in the southern hemisphere: Conformational analysis of enzymatic mannoside hydrolysis informs strategies for enzyme inhibition and inspires solutions to mannoside synthesis. Atomic resolution structures along the reaction coordinate of an inverting alpha-mannosidase show how the enzyme distorts the substrate and transition state. QM/MM calculations reveal how the free energy landscape of isolated alpha-D-mannose is molded on enzyme to only allow one conformationally accessible reaction coordinate.

The reaction coordinate of a bacterial GH47 alpha-mannosidase: a combined quantum mechanical and structural approach.,Thompson AJ, Dabin J, Iglesias-Fernandez J, Ardevol A, Dinev Z, Williams SJ, Bande O, Siriwardena A, Moreland C, Hu TC, Smith DK, Gilbert HJ, Rovira C, Davies GJ Angew Chem Int Ed Engl. 2012 Oct 29;51(44):10997-1001. doi:, 10.1002/anie.201205338. Epub 2012 Sep 26. PMID:23012075<ref>PMID:23012075</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ayo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caulobacter sp. K31]]
[[Category: Large Structures]]
[[Category: Dabin J]]
[[Category: Davies GJ]]
[[Category: Dinev Z]]
[[Category: Gilbert HJ]]
[[Category: Hu TC]]
[[Category: Iglesias-Fernandez A]]
[[Category: Iglesias-Fernandez J]]
[[Category: Moreland C]]
[[Category: Rovira C]]
[[Category: Siriwardena A]]
[[Category: Smith DK]]
[[Category: Thompson AJ]]
[[Category: Williams SJ]]