4i5u: Difference between revisions

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{{STRUCTURE_4i5u| PDB=4i5u | SCENE= }}
==Crystal structure of a fungal chimeric cellobiohydrolase Cel6A==
===Crystal structure of a fungal chimeric cellobiohydrolase Cel6A===
<StructureSection load='4i5u' size='340' side='right' caption='[[4i5u]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
{{ABSTRACT_PUBMED_23404363}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4i5u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I5U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i5r|4i5r]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">avi2, cel6A, cbh2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 ATCC 16454])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </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=4i5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i5u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i5u RCSB], [http://www.ebi.ac.uk/pdbsum/4i5u PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thermostability is an important feature in industrial enzymes: it increases biocatalyst lifetime and enables reactions at higher temperatures, where faster rates and other advantages ultimately reduce the cost of biocatalysis. Here we report the thermostabilization of a chimeric fungal family 6 cellobiohydrolase (HJPlus) by directed evolution using random mutagenesis and recombination of beneficial mutations. Thermostable variant 3C6P has a half-life of 280 min at 75 degrees C and a T50 of 80.1 degrees C, a approximately 15 degrees C increase over the thermostable Cel6A from Humicola insolens (HiCel6A) and a approximately 20 degrees C increase over that from Hypocrea jecorina (HjCel6A). Most of the mutations also stabilize the less-stable HjCel6A, the wild-type Cel6A closest in sequence to 3C6P. During a 60-h Avicel hydrolysis, 3C6P released 2.4 times more cellobiose equivalents at its optimum temperature (Topt ) of 75 degrees C than HiCel6A at its Topt of 60 degrees C. The total cellobiose equivalents released by HiCel6A at 60 degrees C after 60 h is equivalent to the total released by 3C6P at 75 degrees C after approximately 6 h, a 10-fold reduction in hydrolysis time. A binary mixture of thermostable Cel6A and Cel7A hydrolyzes Avicel synergistically and released 1.8 times more cellobiose equivalents than the wild-type mixture, both mixtures assessed at their respective Topt . Crystal structures of HJPlus and 3C6P, determined at 1.5 and 1.2 A resolution, indicate that the stabilization comes from improved hydrophobic interactions and restricted loop conformations by introduced proline residues. Biotechnol. Bioeng. (c) 2013 Wiley Periodicals, Inc.


==Function==
Engineered thermostable fungal Cel6A and Cel7A cellobiohydrolases hydrolyze cellulose efficiently at elevated temperatures.,Wu I, Arnold FH Biotechnol Bioeng. 2013 Feb 12. doi: 10.1002/bit.24864. PMID:23404363<ref>PMID:23404363</ref>
[[http://www.uniprot.org/uniprot/GUX6_HUMIN GUX6_HUMIN]] Plays a central role in the recycling of plant biomass. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.<ref>PMID:9882628</ref>


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4i5u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I5U OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023404363</ref><references group="xtra"/><references/>
__TOC__
[[Category: Arnold, F H.]]
</StructureSection>
[[Category: Wu, I.]]
[[Category: Atcc 16454]]
[[Category: Arnold, F H]]
[[Category: Wu, I]]
[[Category: Cellobiohydrolase]]
[[Category: Cellobiohydrolase]]
[[Category: Chimera protein]]
[[Category: Chimera protein]]
[[Category: Glycoside hydrolase]]
[[Category: Glycoside hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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