5xjh

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'''Unreleased structure'''
 
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The entry 5xjh is ON HOLD until Paper Publication
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==Crystal strcuture of PETase from Ideonella sakaiensis==
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<StructureSection load='5xjh' size='340' side='right' caption='[[5xjh]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xjh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XJH FirstGlance]. <br>
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</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>
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<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=5xjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjh OCA], [http://pdbe.org/5xjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjh RCSB], [http://www.ebi.ac.uk/pdbsum/5xjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjh ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plastics, including poly(ethylene terephthalate) (PET), possess many desirable characteristics and thus are widely used in daily life. However, non-biodegradability, once thought to be an advantage offered by plastics, is causing major environmental problem. Recently, a PET-degrading bacterium, Ideonella sakaiensis, was identified and suggested for possible use in degradation and/or recycling of PET. However, the molecular mechanism of PET degradation is not known. Here we report the crystal structure of I. sakaiensis PETase (IsPETase) at 1.5 A resolution. IsPETase has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate (MHET) moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested. Moreover, other PETase candidates potentially having high PET-degrading activities are suggested based on phylogenetic tree analysis of 69 PETase-like proteins.
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Authors: Joo, S., Kim, K.-J.
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Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation.,Joo S, Cho IJ, Seo H, Son HF, Sagong HY, Shin TJ, Choi SY, Lee SY, Kim KJ Nat Commun. 2018 Jan 26;9(1):382. doi: 10.1038/s41467-018-02881-1. PMID:29374183<ref>PMID:29374183</ref>
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Description: Crystal strcuture of PETase from Ideonella sakaiensis
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kim, K.-J]]
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<div class="pdbe-citations 5xjh" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Joo, S]]
[[Category: Joo, S]]
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[[Category: Kim, K J]]
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[[Category: Hydrolase]]

Revision as of 06:30, 15 February 2018

Crystal strcuture of PETase from Ideonella sakaiensis

5xjh, resolution 1.54Å

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