View source for 5jug


==Structure of an inactive (E45Q) variant of a beta-1,4-mannanase, SsGH134, in complex with Man5==
<StructureSection load='5jug' size='340' side='right'caption='[[5jug]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jug]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._NRRL_B-16215 Streptomyces sp. NRRL B-16215]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JUG 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]] 0.96&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=5jug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jug OCA], [https://pdbe.org/5jug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jug RCSB], [https://www.ebi.ac.uk/pdbsum/5jug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jug ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1L1QK16_9ACTN A0A1L1QK16_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jug" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. NRRL B-16215]]
[[Category: Davies GJ]]
[[Category: Goddard-Borger ED]]
[[Category: Jin Y]]
[[Category: Petricevic M]]
[[Category: Williams SJ]]