3wq7: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vgi|3vgi]], [[3wq0|3wq0]], [[3wq1|3wq1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vgi|3vgi]], [[3wq0|3wq0]], [[3wq1|3wq1]]</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='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=3wq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wq7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wq7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wq7 PDBsum]</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=3wq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wq7 OCA], [http://pdbe.org/3wq7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wq7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wq7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
The hyperthermophilic glycoside hydrolase family endocellulase 12 from the archaeon Pyrococcus furiosus (EGPf; Gene ID PF0854; EC 3.2.1.4) catalyzes the hydrolytic cleavage of the beta-1,4-glucosidic linkage in beta-glucan in lignocellulose biomass. A crystal of EGPf was previously prepared at pH 9.0 and its structure was determined at an atomic resolution of 1.07 A. This article reports the crystallization of EGPf at the more physiologically relevant pH of 5.5. Structure determination showed that this new crystal form has the symmetry of space group C2. Two molecules of the enzyme are observed in the asymmetric unit. Crystal packing is weak at pH 5.5 owing to two flexible interfaces between symmetry-related molecules. Comparison of the EGPf structures obtained at pH 9.0 and pH 5.5 reveals a significant conformational difference at the active centre and in the surface loops. The interfaces in the vicinity of the flexible surface loops impact the quality of the EGPf crystal. | |||
A new crystal form of a hyperthermophilic endocellulase.,Kataoka M, Ishikawa K Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):878-83. doi:, 10.1107/S2053230X14010930. Epub 2014 Jun 18. PMID:25005081<ref>PMID:25005081</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 3wq7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:24, 9 December 2015
New crystal form of the hyperthermophilic family 12 endo-cellulase from Pyrococcus furiosusNew crystal form of the hyperthermophilic family 12 endo-cellulase from Pyrococcus furiosus
Structural highlights
Publication Abstract from PubMedThe hyperthermophilic glycoside hydrolase family endocellulase 12 from the archaeon Pyrococcus furiosus (EGPf; Gene ID PF0854; EC 3.2.1.4) catalyzes the hydrolytic cleavage of the beta-1,4-glucosidic linkage in beta-glucan in lignocellulose biomass. A crystal of EGPf was previously prepared at pH 9.0 and its structure was determined at an atomic resolution of 1.07 A. This article reports the crystallization of EGPf at the more physiologically relevant pH of 5.5. Structure determination showed that this new crystal form has the symmetry of space group C2. Two molecules of the enzyme are observed in the asymmetric unit. Crystal packing is weak at pH 5.5 owing to two flexible interfaces between symmetry-related molecules. Comparison of the EGPf structures obtained at pH 9.0 and pH 5.5 reveals a significant conformational difference at the active centre and in the surface loops. The interfaces in the vicinity of the flexible surface loops impact the quality of the EGPf crystal. A new crystal form of a hyperthermophilic endocellulase.,Kataoka M, Ishikawa K Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):878-83. doi:, 10.1107/S2053230X14010930. Epub 2014 Jun 18. PMID:25005081[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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