4pse: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor== | ==Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor== | ||
<StructureSection load='4pse' size='340' side='right' caption='[[4pse]], [[Resolution|resolution]] 1.71Å' scene=''> | <StructureSection load='4pse' size='340' side='right' caption='[[4pse]], [[Resolution|resolution]] 1.71Å' scene=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=C11:UNDECYL-PHOSPHINIC+ACID+BUTYL+ESTER'>C11</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=C11:UNDECYL-PHOSPHINIC+ACID+BUTYL+ESTER'>C11</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4psc|4psc]], [[4psd|4psd]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4psc|4psc]], [[4psd|4psd]]</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=4pse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pse OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pse RCSB], [http://www.ebi.ac.uk/pdbsum/4pse 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=4pse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pse OCA], [http://pdbe.org/4pse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pse RCSB], [http://www.ebi.ac.uk/pdbsum/4pse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pse ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 15: | Line 16: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4pse" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:00, 4 January 2017
Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitorTrichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor
Structural highlights
Publication Abstract from PubMedCutinases belong to the alpha/beta-hydrolase fold family of enzymes and degrade cutin and various esters, including triglycerides, phospholipids and galactolipids. Cutinases are able to degrade aggregated and soluble substrates because, in contrast with true lipases, they do not have a lid covering their catalytic machinery. We report here the structure of a cutinase from the fungus Trichoderma reesei (Tr) in native and inhibitor-bound conformations, along with its enzymatic characterization. A rare characteristic of Tr cutinase is its optimal activity at acidic pH. Furthermore, Tr cutinase, in contrast with classical cutinases, possesses a lid covering its active site and requires the presence of detergents for activity. In addition to the presence of the lid, the core of the Tr enzyme is very similar to other cutinase cores, with a central five-stranded beta-sheet covered by helices on either side. The catalytic residues form a catalytic triad involving Ser164, His229 and Asp216 that is covered by the two N-terminal helices, which form the lid. This lid opens in the presence of surfactants, such as beta-octylglucoside, and uncovers the catalytic crevice, allowing a C11Y4 phosphonate inhibitor to bind to the catalytic serine. Taken together, these results reveal Tr cutinase to be a member of a new group of lipolytic enzymes resembling cutinases but with kinetic and structural features of true lipases and a heightened specificity for long-chain triglycerides. A Cutinase from Trichoderma reesei with a Lid-Covered Active Site and Kinetic Properties of True Lipases.,Roussel A, Amara S, Nyyssola A, Mateos-Diaz E, Blangy S, Kontkanen H, Westerholm-Parvinen A, Carriere F, Cambillau C J Mol Biol. 2014 Sep 16. pii: S0022-2836(14)00473-2. doi:, 10.1016/j.jmb.2014.09.003. PMID:25219509[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||