3wc3: Difference between revisions
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==Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida== | |||
=== | <StructureSection load='3wc3' size='340' side='right' caption='[[3wc3]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wc3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eisenia_fetida Eisenia fetida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WC3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EF-EG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6396 Eisenia fetida])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wc3 RCSB], [http://www.ebi.ac.uk/pdbsum/3wc3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The saccharification process is essential for bioethanol production from woody biomass including celluloses. Cold-adapted cellulase, which has sufficient activity at low temperature (<293 K), is capable of reducing heating costs during the saccharification process and is suitable for simultaneous saccharification and fermentation. Endo-1,4-beta-glucanase from the earthworm Eisenia fetida (EF-EG2) belonging to glycoside hydrolase family 9 has been shown to have the highest activity at 313 K, and also retained a comparatively high activity at 283 K. The recombinant EF-EG2 was purified expressed in Pichia pastoris, and then grew needle-shaped crystals with dimensions of 0.02 x 0.02 x 1 mm. The crystals belonged to the space group P3221 with unit-cell parameters of a = b = 136 A, c = 55.0 A. The final model of EF-EG2, including 435 residues, two ions, seven crystallization reagents and 696 waters, was refined to a crystallographic R-factor of 14.7% (free R-factor of 16.8%) to 1.5 A resolution. The overall structure of EF-EG2 has an (alpha/alpha)6 barrel fold which contains a putative active-site cleft and a negatively charged surface. This structural information helps us understand the catalytic and cold adaptation mechanisms of EF-EG2. | |||
Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida.,Arimori T, Ito A, Nakazawa M, Ueda M, Tamada T J Synchrotron Radiat. 2013 Nov;20(Pt 6):884-9. doi: 10.1107/S0909049513021110., Epub 2013 Oct 1. PMID:24121333<ref>PMID:24121333</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Glucanase|Glucanase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Eisenia fetida]] | [[Category: Eisenia fetida]] | ||
[[Category: Arimori, T | [[Category: Arimori, T]] | ||
[[Category: Tamada, T | [[Category: Tamada, T]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Sugar binding]] | [[Category: Sugar binding]] | ||
Revision as of 09:50, 21 December 2014
Crystal structure of endo-1,4-beta-glucanase from Eisenia fetida
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