7qjq: Difference between revisions

Revision as of 08:47, 28 December 2022

Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)

Structural highlights

7qjq is a 6 chain structure with sequence from Thermobifida fusca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	PEG
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PETH2_THEFU Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

References

↑ Kleeberg I, Welzel K, Vandenheuvel J, Muller RJ, Deckwer WD. Characterization of a new extracellular hydrolase from Thermobifida fusca degrading aliphatic-aromatic copolyesters. Biomacromolecules. 2005 Jan-Feb;6(1):262-70. doi: 10.1021/bm049582t. PMID:15638529 doi:https://dx.doi.org/10.1021/bm049582t
↑ Huang YC, Chen GH, Chen YF, Chen WL, Yang CH. Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides. Biochem Biophys Res Commun. 2010 Oct 1;400(4):718-23. doi:, 10.1016/j.bbrc.2010.08.136. Epub 2010 Sep 9. PMID:20816933 doi:https://dx.doi.org/10.1016/j.bbrc.2010.08.136
↑ Hegde K, Veeranki VD. Production optimization and characterization of recombinant cutinases from Thermobifida fusca sp. NRRL B-8184. Appl Biochem Biotechnol. 2013 Jun;170(3):654-75. doi: 10.1007/s12010-013-0219-x. , Epub 2013 Apr 19. PMID:23604968 doi:https://dx.doi.org/10.1007/s12010-013-0219-x
↑ Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N. Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca. Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714 doi:https://dx.doi.org/10.1007/s00253-014-5672-0
↑ Then J, Wei R, Oeser T, Barth M, Belisario-Ferrari MR, Schmidt J, Zimmermann W. Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca. Biotechnol J. 2015 Apr;10(4):592-8. doi: 10.1002/biot.201400620. Epub 2015 Jan, 19. PMID:25545638 doi:https://dx.doi.org/10.1002/biot.201400620
↑ Furukawa M, Kawakami N, Tomizawa A, Miyamoto K. Efficient Degradation of Poly(ethylene terephthalate) with Thermobifida fusca Cutinase Exhibiting Improved Catalytic Activity Generated using Mutagenesis and Additive-based Approaches. Sci Rep. 2019 Nov 5;9(1):16038. doi: 10.1038/s41598-019-52379-z. PMID:31690819 doi:https://dx.doi.org/10.1038/s41598-019-52379-z
↑ Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, Kamionka E, Desrousseaux ML, Texier H, Gavalda S, Cot M, Guemard E, Dalibey M, Nomme J, Cioci G, Barbe S, Chateau M, Andre I, Duquesne S, Marty A. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020 Apr;580(7802):216-219. doi: 10.1038/s41586-020-2149-4. Epub 2020 Apr, 8. PMID:32269349 doi:https://dx.doi.org/10.1038/s41586-020-2149-4
↑ Huang YC, Chen GH, Chen YF, Chen WL, Yang CH. Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides. Biochem Biophys Res Commun. 2010 Oct 1;400(4):718-23. doi:, 10.1016/j.bbrc.2010.08.136. Epub 2010 Sep 9. PMID:20816933 doi:https://dx.doi.org/10.1016/j.bbrc.2010.08.136

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Kleeberg I, Welzel K, Vandenheuvel J, Muller RJ, Deckwer WD. Characterization of a new extracellular hydrolase from Thermobifida fusca degrading aliphatic-aromatic copolyesters. Biomacromolecules. 2005 Jan-Feb;6(1):262-70. doi: 10.1021/bm049582t. PMID:15638529 doi:https://dx.doi.org/10.1021/bm049582t

[2] Huang YC, Chen GH, Chen YF, Chen WL, Yang CH. Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides. Biochem Biophys Res Commun. 2010 Oct 1;400(4):718-23. doi:, 10.1016/j.bbrc.2010.08.136. Epub 2010 Sep 9. PMID:20816933 doi:https://dx.doi.org/10.1016/j.bbrc.2010.08.136

[3] Hegde K, Veeranki VD. Production optimization and characterization of recombinant cutinases from Thermobifida fusca sp. NRRL B-8184. Appl Biochem Biotechnol. 2013 Jun;170(3):654-75. doi: 10.1007/s12010-013-0219-x. , Epub 2013 Apr 19. PMID:23604968 doi:https://dx.doi.org/10.1007/s12010-013-0219-x

[4] Roth C, Wei R, Oeser T, Then J, Follner C, Zimmermann W, Strater N. Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca. Appl Microbiol Biotechnol. 2014 Apr 13. PMID:24728714 doi:https://dx.doi.org/10.1007/s00253-014-5672-0

[5] Then J, Wei R, Oeser T, Barth M, Belisario-Ferrari MR, Schmidt J, Zimmermann W. Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca. Biotechnol J. 2015 Apr;10(4):592-8. doi: 10.1002/biot.201400620. Epub 2015 Jan, 19. PMID:25545638 doi:https://dx.doi.org/10.1002/biot.201400620

[6] Furukawa M, Kawakami N, Tomizawa A, Miyamoto K. Efficient Degradation of Poly(ethylene terephthalate) with Thermobifida fusca Cutinase Exhibiting Improved Catalytic Activity Generated using Mutagenesis and Additive-based Approaches. Sci Rep. 2019 Nov 5;9(1):16038. doi: 10.1038/s41598-019-52379-z. PMID:31690819 doi:https://dx.doi.org/10.1038/s41598-019-52379-z

[7] Tournier V, Topham CM, Gilles A, David B, Folgoas C, Moya-Leclair E, Kamionka E, Desrousseaux ML, Texier H, Gavalda S, Cot M, Guemard E, Dalibey M, Nomme J, Cioci G, Barbe S, Chateau M, Andre I, Duquesne S, Marty A. An engineered PET depolymerase to break down and recycle plastic bottles. Nature. 2020 Apr;580(7802):216-219. doi: 10.1038/s41586-020-2149-4. Epub 2020 Apr, 8. PMID:32269349 doi:https://dx.doi.org/10.1038/s41586-020-2149-4

[8] Huang YC, Chen GH, Chen YF, Chen WL, Yang CH. Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides. Biochem Biophys Res Commun. 2010 Oct 1;400(4):718-23. doi:, 10.1016/j.bbrc.2010.08.136. Epub 2010 Sep 9. PMID:20816933 doi:https://dx.doi.org/10.1016/j.bbrc.2010.08.136

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7qjq is ON HOLD  until Paper Publication
+==Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)==
+<StructureSection load='7qjq' size='340' side='right'caption='[[7qjq]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7qjq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJQ FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjq OCA], [https://pdbe.org/7qjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjq RCSB], [https://www.ebi.ac.uk/pdbsum/7qjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Thermobifida fusca]]
+[[Category: Avilan L]]
+[[Category: Beckham GT]]
+[[Category: Gill RS]]
+[[Category: McGeehan JE]]
+[[Category: Zahn M]]

7qjq: Difference between revisions

Revision as of 08:47, 28 December 2022

Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)

Structural highlights

Function

References

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