5luk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a double variant of cutinase 2 from Thermobifida cellulosilytica== | |
| + | <StructureSection load='5luk' size='340' side='right' caption='[[5luk]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5luk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5luk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5luk OCA], [http://pdbe.org/5luk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5luk RCSB], [http://www.ebi.ac.uk/pdbsum/5luk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5luk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have investigated the structures of two native cutinases from Thermobifida cellulosilytica, namely Thc_Cut1 and Thc_Cut2 as well as of two variants, Thc_Cut2_DM (Thc_Cut2_ Arg29Asn_Ala30Val) and Thc_Cut2_TM (Thc_Cut2_Arg19Ser_Arg29Asn_Ala30Val). The four enzymes showed different activities towards the aliphatic polyester poly(lactic acid) (PLLA). The crystal structures of the four enzymes were successfully solved and in combination with Small Angle X-Ray Scattering (SAXS) the structural features responsible for the selectivity difference were elucidated. Analysis of the crystal structures did not indicate significant conformational differences among the different cutinases. However, the distinctive SAXS scattering data collected from the enzymes in solution indicated a remarkable surface charge difference. The difference in the electrostatic and hydrophobic surface properties could explain potential alternative binding modes of the four cutinases on PLLA explaining their distinct activities. This article is protected by copyright. All rights reserved. | ||
| - | + | Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica.,Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263<ref>PMID:28671263</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5luk" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Gruber, K]] | [[Category: Gruber, K]] | ||
| + | [[Category: Hromic, A]] | ||
[[Category: Lyskowski, A]] | [[Category: Lyskowski, A]] | ||
| + | [[Category: Alpha/beta hydrolase]] | ||
| + | [[Category: Cutinase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 09:06, 9 August 2017
Structure of a double variant of cutinase 2 from Thermobifida cellulosilytica
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