View source for 9hyd


==PETaseSM14 from marine-sponge Streptomyces sp.==
<StructureSection load='9hyd' size='340' side='right'caption='[[9hyd]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hyd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Streptomyces Unclassified Streptomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HYD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.425&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9hyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hyd OCA], [https://pdbe.org/9hyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hyd RCSB], [https://www.ebi.ac.uk/pdbsum/9hyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hyd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A679PDB4_9ACTN A0A679PDB4_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The recent discovery of the PETase enzyme family offers a sustainable solution for depolymerizing poly-(ethylene terephthalate) (PET), one of the most widespread plastic compounds, under mild conditions. This enables the environmentally beneficial conversion of plastic waste into value-added products. Among this enzyme family, PETase from Ideonella sakaiensis has been the most extensively studied. Although other similar enzymes have been discovered, our knowledge about the catalytic and structural properties of this class remains limited. In this study, a PETase-like enzyme (PETase SM14) from Streptomyces sp. SM14 was heterologously produced in Escherichia coli, and its activity was tested on post-consumer plastic substrates using high-performance liquid chromatography for product quantification as well as scanning electron microscopy and atomic force microscopy for substrate surface imaging evaluation. PETase SM14 exhibited high salt tolerance (1.5 M), good heat resistance (Tm 56.26 degrees C), and optimal activity at pH 9.0, highlighting its potential for PET waste bioremediation. Furthermore, its X-ray crystal structure was solved at 1.43 A resolution, revealing conserved features of the PETase family with potential relevance for future engineering applications.

Functional and Structural Characterization of PETase SM14 from Marine-Sponge Streptomyces sp. Active on Polyethylene Terephthalate.,Carletti A, Bhattacharya S, Pedroni S, Berto M, Bonettini R, Castagna R, Parisini E, Di Rocco G ACS Sustain Chem Eng. 2025 May 15;13(20):7460-7468. doi: , 10.1021/acssuschemeng.5c00737. eCollection 2025 May 26. PMID:40443410<ref>PMID:40443410</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hyd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Unclassified Streptomyces]]
[[Category: Bhattacharya S]]
[[Category: Castagna R]]
[[Category: Parisini E]]