5yfe
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis== | ==Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis== | ||
| - | <StructureSection load='5yfe' size='340' side='right' caption='[[5yfe]], [[Resolution|resolution]] 1.39Å' scene=''> | + | <StructureSection load='5yfe' size='340' side='right'caption='[[5yfe]], [[Resolution|resolution]] 1.39Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5yfe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YFE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yfe]] 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=5YFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YFE FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5yfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yfe OCA], [http://pdbe.org/5yfe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yfe RCSB], [http://www.ebi.ac.uk/pdbsum/5yfe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yfe 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=5yfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yfe OCA], [http://pdbe.org/5yfe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yfe RCSB], [http://www.ebi.ac.uk/pdbsum/5yfe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yfe ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis. | ||
| + | |||
| + | Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis.,Liu B, He L, Wang L, Li T, Li C, Liu H, Luo Y, Bao R Chembiochem. 2018 Mar 30. doi: 10.1002/cbic.201800097. PMID:29603535<ref>PMID:29603535</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5yfe" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Idesa]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bao, R]] | [[Category: Bao, R]] | ||
[[Category: He, L H]] | [[Category: He, L H]] | ||
Revision as of 07:41, 10 April 2019
Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis
| |||||||||||
Categories: Idesa | Large Structures | Bao, R | He, L H | Liu, B | Hydrolase | Pet degradation
