9knk

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Current revision (17:12, 9 July 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9knk is ON HOLD until 2026-11-19
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==Crystal structure of full-length PHA synthase (PhaC) from Aeromonas caviae==
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<StructureSection load='9knk' size='340' side='right'caption='[[9knk]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9knk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_caviae Aeromonas caviae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KNK 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]] 3.29&#8491;</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=9knk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9knk OCA], [https://pdbe.org/9knk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9knk RCSB], [https://www.ebi.ac.uk/pdbsum/9knk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9knk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O32471_AERCA O32471_AERCA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Polyhydroxyalkanoate (PHA) is a biodegradable polyester that can serve as a promising alternative to petrochemical plastics, which present a serious source of pollution. PHA synthase (PhaC) is a key enzyme responsible for producing a wide variety of PHAs in microorganisms. Here, we present crystal structures of full-length PhaC from Aeromonas caviae, a high-performance PhaC employed for industrial use. The structure reveals an N-terminal helical domain that mediates head-to-head dimerization and stabilizes the C-terminal alpha/beta catalytic domain to form a tunnel that connects the catalytic center embedded inside the protein to the protein surface. We showed that this tunnel is a putative egress tunnel for the product PHA chain. Our results establish a fundamental understanding of the PhaC machinery that should lead to improvement of this enzyme in industrial applications.
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Authors:
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Structures of Polyhydroxyalkanoate Synthase PhaC from Aeromonas caviae, Producing Biodegradable Plastics.,Chek MF, Kim SY, Mori T, Matsumoto K, Sato S, Hakoshima T Angew Chem Int Ed Engl. 2025 Apr 25:e202504626. doi: 10.1002/anie.202504626. PMID:40276819<ref>PMID:40276819</ref>
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Description:
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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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<div class="pdbe-citations 9knk" 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>
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[[Category: Aeromonas caviae]]
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[[Category: Large Structures]]
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[[Category: Chek MF]]
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[[Category: Hakoshima T]]
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[[Category: Kim SY]]
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[[Category: Mori T]]

Current revision

Crystal structure of full-length PHA synthase (PhaC) from Aeromonas caviae

PDB ID 9knk

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