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==Crystal structure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose==
==Crystal structure of the GH2 exo-beta-mannanase from Xanthomonas axonopodis pv. citri in complex with mannose==
<StructureSection load='6bye' size='340' side='right' caption='[[6bye]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
<StructureSection load='6bye' size='340' side='right'caption='[[6bye]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6bye]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanac Xanac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BYE FirstGlance]. <br>
<table><tr><td colspan='2'>[[6bye]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri_pv._citri_str._306 Xanthomonas citri pv. citri str. 306]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BYE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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]] 2.126&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XAC3075 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=190486 XANAC])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene></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=6bye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bye OCA], [http://pdbe.org/6bye PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bye RCSB], [http://www.ebi.ac.uk/pdbsum/6bye PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bye ProSAT]</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=6bye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bye OCA], [https://pdbe.org/6bye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bye RCSB], [https://www.ebi.ac.uk/pdbsum/6bye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bye ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q8PI23_XANAC Q8PI23_XANAC]
The classical microbial strategy for depolymerization of beta-mannan polysaccharides involves the synergistic action of at least two enzymes, endo-1,4-beta-mannanases and beta-mannosidases. In this work, we describe the first exo-beta-mannanase from the GH2 family, isolated from Xanthomonas axonopodis pv. citri (XacMan2A), which can efficiently hydrolyze both manno-oligosaccharides and beta-mannan into mannose. It represents a valuable process simplification in the microbial carbon uptake that could be of potential industrial interest. Biochemical assays revealed a progressive increase in the hydrolysis rates from mannobiose to mannohexaose, which distinguishes XacMan2A from the known GH2 beta-mannosidases. Crystallographic analysis indicates that the active-site topology of XacMan2A underwent profound structural changes at the positive-subsite region, by the removal of the physical barrier canonically observed in GH2 beta-mannosidases, generating a more open and accessible active site with additional productive positive subsites. Besides that, XacMan2A contains two residue substitutions in relation to typical GH2 beta-mannosidases, Gly(439) and Gly(556), which alter the active site volume and are essential to its mode of action. Interestingly, the only other mechanistically characterized mannose-releasing exo-beta-mannanase so far is from the GH5 family, and its mode of action was attributed to the emergence of a blocking loop at the negative-subsite region of a cleft-like active site, whereas in XacMan2A, the same activity can be explained by the removal of steric barriers at the positive-subsite region in an originally pocket-like active site. Therefore, the GH2 exo-beta-mannanase represents a distinct molecular route to this rare activity, expanding our knowledge about functional convergence mechanisms in carbohydrate-active enzymes.
 
Structural basis of exo-beta-mannanase activity in the GH2 family.,Domingues MN, Souza FHM, Vieira PS, de Morais MAB, Zanphorlin LM, Dos Santos CR, Pirolla RAS, Honorato RV, de Oliveira PSL, Gozzo FC, Murakami MT J Biol Chem. 2018 Aug 31;293(35):13636-13649. doi: 10.1074/jbc.RA118.002374. Epub, 2018 Jul 11. PMID:29997257<ref>PMID:29997257</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bye" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Mannosidase|Mannosidase]]
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Xanac]]
[[Category: Large Structures]]
[[Category: Domingues, M N]]
[[Category: Xanthomonas citri pv. citri str. 306]]
[[Category: Morais, M A.B]]
[[Category: Domingues MN]]
[[Category: Murakami, M T]]
[[Category: Morais MAB]]
[[Category: Vieira, P S]]
[[Category: Murakami MT]]
[[Category: Carbohydrate]]
[[Category: Vieira PS]]
[[Category: Hydrolase-carbohydrate complex]]
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