5lui

From Proteopedia

Structure of cutinase 1 from Thermobifida cellulosilytica

PDB ID 5lui

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Structural highlights

5lui is a 1 chain structure with sequence from Thermobifida cellulosilytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PETH1_THECS Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.1). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.1, PubMed:23718548, PubMed:23592055). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.1, PubMed:23718548, PubMed:23592055). Capable of degrading the bioplastic poly(lactic acid) (PLLA) (PubMed:28671263).^[1] ^[2] ^[3] [UniProtKB:A0A0K8P6T7]

Publication Abstract from PubMed

We have investigated the structures of two native cutinases from Thermobifida cellulosilytica, namely Thc_Cut1 and Thc_Cut2 as well as of two variants, Thc_Cut2_DM (Thc_Cut2_ Arg29Asn_Ala30Val) and Thc_Cut2_TM (Thc_Cut2_Arg19Ser_Arg29Asn_Ala30Val). The four enzymes showed different activities towards the aliphatic polyester poly(lactic acid) (PLLA). The crystal structures of the four enzymes were successfully solved and in combination with Small Angle X-Ray Scattering (SAXS) the structural features responsible for the selectivity difference were elucidated. Analysis of the crystal structures did not indicate significant conformational differences among the different cutinases. However, the distinctive SAXS scattering data collected from the enzymes in solution indicated a remarkable surface charge difference. The difference in the electrostatic and hydrophobic surface properties could explain potential alternative binding modes of the four cutinases on PLLA explaining their distinct activities. This article is protected by copyright. All rights reserved.

Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica.,Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Herrero Acero E, Ribitsch D, Dellacher A, Zitzenbacher S, Marold A, Steinkellner G, Gruber K, Schwab H, Guebitz GM. Surface engineering of a cutinase from Thermobifida cellulosilytica for improved polyester hydrolysis. Biotechnol Bioeng. 2013 Oct;110(10):2581-90. doi: 10.1002/bit.24930. Epub 2013 , Apr 29. PMID:23592055 doi:http://dx.doi.org/10.1002/bit.24930
↑ Ribitsch D, Yebra AO, Zitzenbacher S, Wu J, Nowitsch S, Steinkellner G, Greimel K, Doliska A, Oberdorfer G, Gruber CC, Gruber K, Schwab H, Stana-Kleinschek K, Acero EH, Guebitz GM. Fusion of binding domains to Thermobifida cellulosilytica cutinase to tune sorption characteristics and enhancing PET hydrolysis. Biomacromolecules. 2013 Jun 10;14(6):1769-76. PMID:23718548 doi:10.1021/bm400140u
↑ Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM. Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica. Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263 doi:http://dx.doi.org/10.1002/bit.26372
↑ Ribitsch D, Hromic A, Zitzenbacher S, Zartl B, Gamerith C, Pellis A, Jungbauer A, Lyskowski A, Steinkellner G, Gruber K, Tscheliessnig R, Acero EH, Guebitz GM. Small cause, large effect: Structural characterization of cutinases from Thermobifida cellulosilytica. Biotechnol Bioeng. 2017 Jul 3. doi: 10.1002/bit.26372. PMID:28671263 doi:http://dx.doi.org/10.1002/bit.26372