2czq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==A novel cutinase-like protein from Cryptococcus sp.== | ==A novel cutinase-like protein from Cryptococcus sp.== | ||
<StructureSection load='2czq' size='340' side='right' caption='[[2czq]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='2czq' size='340' side='right' caption='[[2czq]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
| Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[2czq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptococcus_sp. Cryptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CZQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2czq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryptococcus_sp. Cryptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CZQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=2czq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2czq OCA], [http://pdbe.org/2czq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2czq RCSB], [http://www.ebi.ac.uk/pdbsum/2czq 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=2czq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2czq OCA], [http://pdbe.org/2czq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2czq RCSB], [http://www.ebi.ac.uk/pdbsum/2czq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2czq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 10: | Line 11: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/2czq_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/2czq_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:46, 30 May 2018
A novel cutinase-like protein from Cryptococcus sp.A novel cutinase-like protein from Cryptococcus sp.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity. Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2.,Kodama Y, Masaki K, Kondo H, Suzuki M, Tsuda S, Nagura T, Shimba N, Suzuki E, Iefuji H Proteins. 2009 Nov 15;77(3):710-7. PMID:19544571[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||