8hka

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'''Unreleased structure'''
 
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The entry 8hka is ON HOLD until Paper Publication
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==TPA bound-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis==
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<StructureSection load='8hka' size='340' side='right'caption='[[8hka]], [[Resolution|resolution]] 1.02&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8hka]] 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=8HKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HKA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UB7:terephthalic+acid'>UB7</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=8hka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hka OCA], [https://pdbe.org/8hka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hka RCSB], [https://www.ebi.ac.uk/pdbsum/8hka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hka ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0K8P8D2_IDESA A0A0K8P8D2_IDESA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ideonella sakaiensis is the bacterium that can survive by degrading polyethylene terephthalate (PET) plastic, and terephthalic acid (TPA) binding protein (IsTBP) is an essential periplasmic protein for uptake of TPA into the cytosol for complete degradation of PET. Here, we demonstrated that IsTBP has remarkably high specificity for TPA among 33 monophenolic compounds and two 1,6-dicarboxylic acids tested. Structural comparisons with 6-carboxylic acid binding protein (RpAdpC) and TBP from Comamonas sp. E6 (CsTphC) revealed the key structural features that contribute to high TPA specificity and affinity of IsTBP. We also elucidated the molecular mechanism underlying the conformational change upon TPA binding. In addition, we developed the IsTBP variant with enhanced TPA sensitivity, which can be expanded for the use of TBP as a biosensor for PET degradation.
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Authors: Lee, S.H., Seo, H., Kim, K.-J.
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Molecular mechanism underlying high-affinity terephthalate binding and conformational change of TBP from Ideonella sakaiensis.,Lee SH, Seo H, Hong H, Kim M, Kim KJ Int J Biol Macromol. 2023 Jul 15;243:125252. doi: 10.1016/j.ijbiomac.2023.125252. , Epub 2023 Jun 7. PMID:37295700<ref>PMID:37295700</ref>
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Description: TPA bound-form of Periplasmic terephthalate binding protein (TBP) 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 8hka" style="background-color:#fffaf0;"></div>
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[[Category: Seo, H]]
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== References ==
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[[Category: Lee, S.H]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ideonella sakaiensis]]
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[[Category: Large Structures]]
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[[Category: Kim K-J]]
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[[Category: Lee SH]]
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[[Category: Seo H]]

Revision as of 09:40, 21 June 2023

TPA bound-form of Periplasmic terephthalate binding protein (TBP) from Ideonella sakaiensis

PDB ID 8hka

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