5xh2

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'''Unreleased structure'''
 
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The entry 5xh2 is ON HOLD until Apr 19 2019
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==Crystal structure of a novel PET hydrolase R103G/S131A mutant in complex with pNP from Ideonella sakaiensis 201-F6==
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<StructureSection load='5xh2' size='340' side='right'caption='[[5xh2]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5xh2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ideonella_sakaiensis Ideonella sakaiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XH2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NPO:P-NITROPHENOL'>NPO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xh2 OCA], [https://pdbe.org/5xh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xh2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xh2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PETH_IDESA PETH_IDESA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated.
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Authors: Han, X., Liu, W.D., Zheng, Y.Y., Chen, C.C., Guo, R.T.
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Structural insight into catalytic mechanism of PET hydrolase.,Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT Nat Commun. 2017 Dec 13;8(1):2106. doi: 10.1038/s41467-017-02255-z. PMID:29235460<ref>PMID:29235460</ref>
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Description: Crystal structure of double mutant of a novel esterase with ligand
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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: Han, X]]
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<div class="pdbe-citations 5xh2" style="background-color:#fffaf0;"></div>
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[[Category: Chen, C.C]]
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== References ==
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[[Category: Liu, W.D]]
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<references/>
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[[Category: Guo, R.T]]
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__TOC__
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[[Category: Zheng, Y.Y]]
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</StructureSection>
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[[Category: Ideonella sakaiensis]]
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[[Category: Large Structures]]
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[[Category: Chen CC]]
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[[Category: Guo RT]]
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[[Category: Han X]]
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[[Category: Liu WD]]
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[[Category: Zheng YY]]

Current revision

Crystal structure of a novel PET hydrolase R103G/S131A mutant in complex with pNP from Ideonella sakaiensis 201-F6

PDB ID 5xh2

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