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5jts

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<StructureSection load='5jts' size='340' side='right'caption='[[5jts]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
<StructureSection load='5jts' size='340' side='right'caption='[[5jts]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jts]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chainia_sp. Chainia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JTS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JTS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.09&#8491;</td></tr>
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<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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=5jts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jts OCA], [http://pdbe.org/5jts PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jts RCSB], [http://www.ebi.ac.uk/pdbsum/5jts PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jts ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jts OCA], [https://pdbe.org/5jts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jts RCSB], [https://www.ebi.ac.uk/pdbsum/5jts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jts ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1L1QK12_STRSQ A0A1L1QK12_STRSQ]
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The enzymatic cleavage of beta-1,4-mannans is achieved by endo-beta-1,4-mannanases, enzymes involved in germination of seeds and microbial hemicellulose degradation, and which have increasing industrial and consumer product applications. beta-Mannanases occur in a range of families of the CAZy sequence-based glycoside hydrolase (GH) classification scheme including families 5, 26, and 113. In this work we reveal that beta-mannanases of the newly described GH family 134 differ from other mannanase families in both their mechanism and tertiary structure. A representative GH family 134 endo-beta-1,4-mannanase from a Streptomyces sp. displays a fold closely related to that of hen egg white lysozyme but acts with inversion of stereochemistry. A Michaelis complex with mannopentaose, and a product complex with mannotriose, reveal ligands with pyranose rings distorted in an unusual inverted chair conformation. Ab initio quantum mechanics/molecular mechanics metadynamics quantified the energetically accessible ring conformations and provided evidence in support of a 1C4 --&gt; 3H4double dagger --&gt; 3S1 conformational itinerary along the reaction coordinate. This work, in concert with that on GH family 124 cellulases, reveals how the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner.
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A beta-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism.,Jin Y, Petricevic M, John A, Raich L, Jenkins H, Portela De Souza L, Cuskin F, Gilbert HJ, Rovira C, Goddard-Borger ED, Williams SJ, Davies GJ ACS Cent Sci. 2016 Dec 28;2(12):896-903. doi: 10.1021/acscentsci.6b00232. Epub, 2016 Nov 8. PMID:28058278<ref>PMID:28058278</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5jts" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chainia sp]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mannan endo-1,4-beta-mannosidase]]
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[[Category: Streptomyces sp]]
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[[Category: Davies, G J]]
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[[Category: Davies GJ]]
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[[Category: Goddard-Borger, E D]]
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[[Category: Goddard-Borger ED]]
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[[Category: Jin, Y]]
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[[Category: Jin Y]]
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[[Category: Petricevic, M]]
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[[Category: Petricevic M]]
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[[Category: Williams, S J]]
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[[Category: Williams SJ]]
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[[Category: 4-mannanase]]
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[[Category: Beta-1]]
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[[Category: Carbohydrate degrading]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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Current revision

Structure of a beta-1,4-mannanase, SsGH134.

PDB ID 5jts

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