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  Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction during Vancomycin Biosynthesis

Zerbe, K., Pylypenko, O., Vitali, F., Zhang, W., Rouset, S., Heck, M., et al. (2002). Crystal Structure of OxyB, a Cytochrome P450 Implicated in an Oxidative Phenol Coupling Reaction during Vancomycin Biosynthesis. Journal of Biological Chemistry, 277(49): 1, pp. 47476-47485. Retrieved from http://dx.doi.org/10.1074/jbc.M206342200.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Zerbe, Katja, Author
Pylypenko, Olena1, Author
Vitali, Francesca, Author
Zhang, Weiwen, Author
Rouset, Severine, Author
Heck, Markus, Author
Vrijbloed, Jan W., Author
Bischoff, Daniel, Author
Bister, Bojan, Author
Süssmuth, Roderich D., Author
Pelzer, Stefan, Author
Wohlleben, Wolfgang, Author
Robinson, John A., Author
Schlichting, Ilme2, Author           
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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 Abstract: Gene-inactivation studies point to the involvement of OxyB in catalyzing the first oxidative phenol coupling reaction during glycopeptide antibiotic biosynthesis. The oxyB gene has been cloned and sequenced from the vancomycin producer Amycolatopsis orientalis, and the hemoprotein has been produced in Escherichia coli, crystallized, and its structure determined to 1.7-Å resolution. OxyB gave UV-visible spectra characteristic of a P450-like hemoprotein in the low spin ferric state. After reduction to the ferrous state by dithionite or by spinach ferredoxin and ferredoxin reductase, the CO-ligated form gave a 450-nm peak in a UV-difference spectrum. Addition of putative heptapeptide substrates to resting OxyB produced type I changes to the UV spectrum, but no turnover was observed in the presence of ferredoxin and ferredoxin reductase, showing that either the peptides or the reduction system, or both, are insufficient to support a full catalytic cycle. OxyB exhibits the typical P450-fold, with helix L containing the signature sequence FGHGXHXCLG and Cys347 being the proximal axial thiolate ligand of the heme iron. The structural similarity of OxyB is highest to P450nor, P450terp, CYP119, and P450eryF. In OxyB, the F and G helices are rotated out of the active site compared with P450nor, resulting in a much more open active site, consistent with the larger size of the presumed heptapeptide substrate.

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Language(s): eng - English
 Dates: 2002-12-06
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 21752
URI: http://dx.doi.org/10.1074/jbc.M206342200
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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 277 (49) Sequence Number: 1 Start / End Page: 47476 - 47485 Identifier: -