3x17

<StructureSection load='3x17' size='340' side='right'caption='[[3x17]], [[Resolution|resolution]] 2.15&Aring;' scene=''>

<table><tr><td colspan='2'>[[3x17]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X17 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3x17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x17 OCA], [https://pdbe.org/3x17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x17 RCSB], [https://www.ebi.ac.uk/pdbsum/3x17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x17 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

A metagenome-derived glycoside hydrolase family 9 enzyme with an N-terminal immunoglobulin-like (Ig-like) domain, leaf-branch compost (LC)-CelG, was characterized and its crystal structure was determined. LC-CelG did not hydrolyze p-nitrophenyl cellobioside but hydrolyzed CM-cellulose, indicating that it is endoglucanase. LC-CelG exhibited the highest activity at 70 degrees C and &gt;80% of the maximal activity at a broad pH range of 5-9. Its denaturation temperature was 81.4 degrees C, indicating that LC-CelG is a thermostable enzyme. The structure of LC-CelG resembles those of CelD from Clostridium thermocellum (CtCelD), Cel9A from Alicyclobacillus acidocaldarius (AaCel9A), and cellobiohydrolase CbhA from C. thermocellum (CtCbhA), which show relatively low (29-31%) amino acid sequence identities to LC-CelG. Three acidic active site residues are conserved as Asp194, Asp197, and Glu558 in LC-CelG. Ten of the thirteen residues that form the substrate binding pocket of AaCel9A are conserved in LC-CelG. Removal of the Ig-like domain reduced the activity and stability of LC-CelG by 100-fold and 6.3 degrees C, respectively. Removal of the Gln40- and Asp99-mediated interactions between the Ig-like and catalytic domains destabilized LC-CelG by 5.0 degrees C without significantly affecting its activity. These results suggest that the Ig-like domain contributes to the stabilization of LC-CelG mainly due to the Gln40- and Asp99-mediated interactions. Because the LC-CelG derivative lacking the Ig-like domain accumulated in Escherichia coli cells mostly in an insoluble form and this derivative accumulated in a soluble form exhibited very weak activity, the Ig-like domain may be required to make the conformation of the active site functional and prevent aggregation of the catalytic domain.

Structure, activity, and stability of metagenome-derived glycoside hydrolase family 9 endoglucanase with an N-terminal Ig-like domain.,Okano H, Kanaya E, Ozaki M, Angkawidjaja C, Kanaya S Protein Sci. 2014 Dec 26. doi: 10.1002/pro.2632. PMID:25545469<ref>PMID:25545469</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3x17" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Cellulase]]

[[Category: Angkawidjaja, C]]

[[Category: Kanaya, S]]

[[Category: Okano, H]]

[[Category: Hydrolase]]