View source for 3wdu


==The complex structure of PtLic16A with cellobiose==
<StructureSection load='3wdu' size='340' side='right'caption='[[3wdu]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wdu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paecilomyces_sp._'thermophila' Paecilomyces sp. 'thermophila']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WDU 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</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=3wdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wdu OCA], [https://pdbe.org/3wdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wdu RCSB], [https://www.ebi.ac.uk/pdbsum/3wdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wdu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E0XN39_9EURO E0XN39_9EURO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The thermostable 1,3-1,4-beta-glucanase PtLic16A from the fungus Paecilomyces thermophila catalyzes stringent hydrolysis of barley beta-glucan and lichenan with an outstanding efficiency and has great potential for broad industrial applications. Here, we report the crystal structures of PtLic16A and an inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose at 1.80A to 2.25A resolution. PtLic16A adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. These structures suggest that PtLic16A might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively. Interestingly, in the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration. By combining all crystal structures solved here, a comprehensive binding mode for a substrate is proposed. These findings not only help understand the 1,3-1,4-beta-glucanase catalytic mechanism but also provide a basis for further enzymatic engineering.

Structural and mutagenetic analyses of a 1,3-1,4-beta-glucanase from Paecilomyces thermophila.,Cheng YS, Huang CH, Chen CC, Huang TY, Ko TP, Huang JW, Wu TH, Liu JR, Guo RT Biochim Biophys Acta. 2014 Feb;1844(2):366-73. doi: 10.1016/j.bbapap.2013.11.005., Epub 2013 Nov 18. PMID:24262091<ref>PMID:24262091</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wdu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paecilomyces sp. 'thermophila']]
[[Category: Chen CC]]
[[Category: Cheng YS]]
[[Category: Guo RT]]
[[Category: Huang CH]]
[[Category: Huang JW]]
[[Category: Huang TY]]
[[Category: Ko TP]]
[[Category: Liu JR]]
[[Category: Wu TH]]