3vgi
From Proteopedia
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| - | [[ | + | ==The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus== |
| + | <StructureSection load='3vgi' size='340' side='right' caption='[[3vgi]], [[Resolution|resolution]] 1.07Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3vgi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VGI FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3az0|3az0]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vgi RCSB], [http://www.ebi.ac.uk/pdbsum/3vgi PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of beta-1,4-glucosidic linkage in beta-glucan cellulose. A truncated EGPf (EGPfDeltaN30) mutant lacking the proline and hydroxyl-residue rich region at the N terminus was constructed, and its crystal structure was resolved at an atomic resolution of 1.07 A. Our results indicate that the structure of EGPf, which consists of a beta-jelly roll, exhibits structural similarity with the endocellulase of Thermotoga maritima. Additionally, we further determined that the thermostability of EGPf is maintained in part by the binding of Ca(2)(+) in a DxDxDG Ca(2)(+)-binding motif, atypical of most archaeal proteins. | ||
| - | + | Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus.,Kim HW, Kataoka M, Ishikawa K FEBS Lett. 2012 Apr 5;586(7):1009-13. Epub 2012 Mar 6. PMID:22569255<ref>PMID:22569255</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Ishikawa, K.]] | [[Category: Ishikawa, K.]] | ||
Revision as of 10:26, 16 June 2014
The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus
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