6ilw
From Proteopedia
(Difference between revisions)
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<StructureSection load='6ilw' size='340' side='right'caption='[[6ilw]], [[Resolution|resolution]] 1.57Å' scene=''> | <StructureSection load='6ilw' size='340' side='right'caption='[[6ilw]], [[Resolution|resolution]] 1.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ilw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ILW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ilw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Idesa Idesa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ILW 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=NA:SODIUM+ION'>NA</scene></td></tr> | </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=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ISF6_4831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1547922 IDESA])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(ethylene_terephthalate)_hydrolase Poly(ethylene terephthalate) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.101 3.1.1.101] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(ethylene_terephthalate)_hydrolase Poly(ethylene terephthalate) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.101 3.1.1.101] </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=6ilw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ilw OCA], [http://pdbe.org/6ilw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ilw RCSB], [http://www.ebi.ac.uk/pdbsum/6ilw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ilw ProSAT]</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=6ilw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ilw OCA], [http://pdbe.org/6ilw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ilw RCSB], [http://www.ebi.ac.uk/pdbsum/6ilw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ilw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polyethylene terephthalate (PET) hydrolase from Ideonella sakaiensis (IsPETase) can be used to degrade PET. In order to use IsPETase in industry, we studied the enzymatic activity of IsPETase in different conditions containing environmental and physicochemical factors commonly found in nature. We observed that salts and glycerol enhanced the enzymatic activity, while detergents and organic solvents reduced the enzymatic activity. IsPETase hydrolyzed p-nitrophenyl (p-NP) esters instead of naphthyl esters. To make IsPETase an enzyme capable of hydrolyzing naphthyl esters, site-directed mutagenesis was carried out based on the structural information provided by the crystal structure. We found that the IsPETase(S93M), IsPETase(W159F), and IsPETase(N241F) mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this alpha/beta-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters. | ||
| + | |||
| + | Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.,Liu C, Shi C, Zhu S, Wei R, Yin CC Biochem Biophys Res Commun. 2019 Jan 1;508(1):289-294. doi:, 10.1016/j.bbrc.2018.11.148. Epub 2018 Nov 27. PMID:30502092<ref>PMID:30502092</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ilw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Idesa]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu, C C]] | [[Category: Liu, C C]] | ||
Revision as of 07:52, 10 April 2019
Crystal strcuture of PETase from Ideonella sakaiensis
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