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Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1.
Acta Crystallogr F Struct Biol Commun. 2020 Jul 01; 76(Pt 7):309-313.AC

Abstract

During the microbial degradation of borneol, a bicyclic plant monoterpene, it is first converted into camphor by borneol dehydrogenase (BDH) and then enters a known camphor-degradation pathway. Previously, a recombinant Pseudomonas BDH was found in inclusion bodies when expressed in Escherichia coli. After refolding, it was still unstable and was difficult to concentrate. Here, the protein-expression conditions were improved by changing the medium from lysogeny broth to Terrific Broth, yielding a soluble form of the enzyme with higher activity. The protein was crystallized and its 3D structure was determined by X-ray diffraction. Like other known homologues such as quinuclidinone reductase, the protein forms a tetramer with subunits containing Rossmann folds. Structural comparison revealed major differences in the C-terminal helices and the associated loops. It is likely that these regions contain the determinants for substrate recognition.

Authors+Show Affiliations

Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien 97004, Taiwan.Department of Biochemistry, School of Medicine, Tzu Chi University, Hualien 97004, Taiwan.Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32627746

Citation

Khine, Aye Aye, et al. "Structural Characterization of Borneol Dehydrogenase From Pseudomonas Sp. TCU-HL1." Acta Crystallographica. Section F, Structural Biology Communications, vol. 76, no. Pt 7, 2020, pp. 309-313.
Khine AA, Chen HP, Huang KF, et al. Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1. Acta Crystallogr F Struct Biol Commun. 2020;76(Pt 7):309-313.
Khine, A. A., Chen, H. P., Huang, K. F., & Ko, T. P. (2020). Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1. Acta Crystallographica. Section F, Structural Biology Communications, 76(Pt 7), 309-313. https://doi.org/10.1107/S2053230X20008584
Khine AA, et al. Structural Characterization of Borneol Dehydrogenase From Pseudomonas Sp. TCU-HL1. Acta Crystallogr F Struct Biol Commun. 2020 Jul 1;76(Pt 7):309-313. PubMed PMID: 32627746.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural characterization of borneol dehydrogenase from Pseudomonas sp. TCU-HL1. AU - Khine,Aye Aye, AU - Chen,Hao Ping, AU - Huang,Kai Fa, AU - Ko,Tzu Ping, Y1 - 2020/07/01/ PY - 2020/05/06/received PY - 2020/06/25/accepted PY - 2020/7/7/entrez PY - 2020/7/7/pubmed PY - 2020/7/7/medline KW - NAD KW - Rossmann fold KW - camphor KW - expression medium KW - oxidoreductases KW - plant terpenoids KW - protein solubility SP - 309 EP - 313 JF - Acta crystallographica. Section F, Structural biology communications JO - Acta Crystallogr F Struct Biol Commun VL - 76 IS - Pt 7 N2 - During the microbial degradation of borneol, a bicyclic plant monoterpene, it is first converted into camphor by borneol dehydrogenase (BDH) and then enters a known camphor-degradation pathway. Previously, a recombinant Pseudomonas BDH was found in inclusion bodies when expressed in Escherichia coli. After refolding, it was still unstable and was difficult to concentrate. Here, the protein-expression conditions were improved by changing the medium from lysogeny broth to Terrific Broth, yielding a soluble form of the enzyme with higher activity. The protein was crystallized and its 3D structure was determined by X-ray diffraction. Like other known homologues such as quinuclidinone reductase, the protein forms a tetramer with subunits containing Rossmann folds. Structural comparison revealed major differences in the C-terminal helices and the associated loops. It is likely that these regions contain the determinants for substrate recognition. SN - 2053-230X UR - https://www.unboundmedicine.com/medline/citation/32627746/Structural_characterization_of_borneol_dehydrogenase_from_Pseudomonas_sp._TCU-HL1 L2 - http://scripts.iucr.org/cgi-bin/paper?S2053230X20008584 DB - PRIME DP - Unbound Medicine ER -
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