View source for 5glx


==Crystal structure of a glycoside hydrolase from Thielavia terrestris NRRL 8126==
<StructureSection load='5glx' size='340' side='right'caption='[[5glx]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5glx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothielavioides_terrestris_NRRL_8126 Thermothielavioides terrestris NRRL 8126]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GLX 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]] 1.42&#8491;</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=5glx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5glx OCA], [https://pdbe.org/5glx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5glx RCSB], [https://www.ebi.ac.uk/pdbsum/5glx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5glx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G2QVH7_THETT G2QVH7_THETT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
1,4-beta-Endoglucanase is one of the most important biocatalysts in modern industries. Here, a glycoside hydrolase (GH) family 45 endoglucanase from thermophilic fungus Theilavia terrestris (TtCel45A) was expressed in Pichia pastoris. The recombinant protein shows optimal activity at 60 degrees C, pH 4-5. The enzyme exhibits extraordinary thermostability that more than 80% activity was detected after heating at 80 degrees C for 2.5h. The high resolution crystal structures of apo-form enzyme and that in complex with cellobiose and cellotetraose were solved to 1.36-1.58A. The protein folds into two overall regions: one is a six-stranded beta-barrel, and the other one consists of several extended loops. Between the two regions lies the substrate-binding channel, which is an open cleft spanning across the protein surface. A continuous substrate-binding cleft from subsite -4 to +3 were clearly identified in the complex structures. Notably, the flexible V-VI loop (113Gly-114Gly-115Asp-116Leu-117Gly-118Ser) is found to open in the presence of -1 sugar, with D115 and L116 swung away to yield a space to accommodate the catalytic acid D122 and the 2,5B boat conformation of -1 sugar during transition state. Collectively, we characterized the enzyme properties of P. pastoris-expressed TtCel45A and solved high-resolution crystal structures of the enzyme. These results are of great interests in industrial applications and provide new insights into the fundamental understanding of enzyme catalytic mechanism of GH45 endoglucanases.

Characterization and crystal structure of a thermostable glycoside hydrolase family 45 1,4-beta-endoglucanase from Thielavia terrestris.,Gao J, Huang JW, Li Q, Liu W, Ko TP, Zheng Y, Xiao X, Kuo CJ, Chen CC, Guo RT Enzyme Microb Technol. 2017 Apr;99:32-37. doi: 10.1016/j.enzmictec.2017.01.005., Epub 2017 Jan 17. PMID:28193329<ref>PMID:28193329</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5glx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermothielavioides terrestris NRRL 8126]]
[[Category: Chen CC]]
[[Category: Gao J]]
[[Category: Guo RT]]
[[Category: Liu WD]]
[[Category: Zheng YY]]