4u5i: Difference between revisions
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==Complex structure of mutant CtCel5E (E314A) with xylobiose== | |||
<StructureSection load='4u5i' size='340' side='right'caption='[[4u5i]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4u5i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U5I 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900116:4beta-beta-xylobiose'>PRD_900116</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=4u5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u5i OCA], [https://pdbe.org/4u5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u5i RCSB], [https://www.ebi.ac.uk/pdbsum/4u5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u5i ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GUNH_ACET2 GUNH_ACET2] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We expressed an active form of CtCel5E (a bifunctional cellulase/xylanase from Clostridium thermocellum), performed biochemical characterization, and determinedsolved its apo and ligand-bound crystal structures. From the structures, Asn93, His168, His169, Asn208, Trp347, and Asn349 were shown to provide H-bonding/hydrophobic interactions with both ligands. Compared with to the structures of TmCel5A, a bi-functional cellulase/mannanase homolog from Thermotoga maritima, a flexible loop region in CtCel5E is the key for discriminating substrates. Moreover, site-directed mutagenesis data confirmed that His168 is essential for xylanase activity, His169 is more important for xylanasecellulase activity, Asn349 is only required for cellulase activity, whereas Asn93, Asn208, Tyr270, and Trp347 and Asn349 are critical for both activities. In contrast, F267A improves enzyme activities. | |||
Biochemical characterization and structural analysis of a bi-functional cellulase/xylanase from Clostridium thermocellum.,Yuan SF, Wu TH, Lee HL, Hsieh HY, Lin WL, Yang B, Chang CK, Li Q, Gao J, Huang CH, Ho MC, Guo RT, Liang PH J Biol Chem. 2015 Jan 9. pii: jbc.M114.604454. PMID:25575592<ref>PMID:25575592</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4u5i" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetivibrio thermocellus ATCC 27405]] | |||
[[Category: Large Structures]] | |||
[[Category: Guo RT]] | |||
[[Category: Huang CH]] | |||
[[Category: Wu TH]] | |||
