View source for 9hl5


==Crystal structure of halo-tolerant PETase from marine metagenome (HaloPETase1)==
<StructureSection load='9hl5' size='340' side='right'caption='[[9hl5]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9hl5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HL5 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]] 1.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=9hl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hl5 OCA], [https://pdbe.org/9hl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hl5 RCSB], [https://www.ebi.ac.uk/pdbsum/9hl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hl5 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzymatic degradation of polyethylene terephthalate (PET) offers a sustainable solution for PET recycling. Over the past two decades, more than 100 PETases have been characterized, primarily exhibiting similar sequences and structures. Here, we report PET-degrading alpha/beta hydrolases, including HaloPETase1 from the marine Halopseudomonas lineage, thereby extending the narrow sequence space by novel features at the active site. The crystal structure of HaloPETase1 was determined to a resolution of 1.16 A, revealing a unique active site architecture and a lack of the canonical pi-stacking clamp found in PETases so far. Further, variations in active site composition and loop structures were observed. Additionally, we found five more enzymes from the same lineage, two of which have a high similarity to type IIa bacterial PETases, while the other three resemble HaloPETase1. All these enzymes exhibited high salt tolerance ranging from 2.5 to 5 M NaCl, leading to higher total product releases upon PET degradation at 40 or 50 degrees C. Based on these findings, we propose an extension of the existing PETase classification system to include type III PETases.

A third type of PETase from the marine Halopseudomonas lineage.,Turak O, Gagsteiger A, Upadhyay A, Kriegel M, Salein P, Bohnke-Brandt S, Agarwal S, Borchert E, Hocker B Protein Sci. 2025 Oct;34(10):e70305. doi: 10.1002/pro.70305. PMID:40960396<ref>PMID:40960396</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9hl5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured bacterium]]
[[Category: Hocker B]]
[[Category: Kriegel M]]
[[Category: Turak O]]