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  The structure of a transient complex of a nonribosomal peptide synthetase and a cytochrome P450 monooxygenase

Haslinger, K., Brieke, C., Uhlmann, S., Sieverling, L., Süssmuth, R. D., & Cryle, M. (2014). The structure of a transient complex of a nonribosomal peptide synthetase and a cytochrome P450 monooxygenase. Angewandte Chemie International Edition: a journal of the Gesellschaft Deutscher Chemiker, 53(32), 8518-8522. doi:10.1002/anie.201404977.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-F1B9-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-A432-1
Genre: Journal Article

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AngewChemIntEd_53_2014_1 – 6.pdf (Any fulltext), 2MB
 
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 Creators:
Haslinger, Kristina1, Author              
Brieke, Clara1, Author              
Uhlmann, Stefanie, Author
Sieverling, Lina1, Author              
Süssmuth, Roderich D., Author
Cryle, Max1, 2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Cytochrome P450, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497697              

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Free keywords: bioorganic chemistry; biosynthesis; metalloenzymes; protein–protein interactions; structural biology
 Abstract: Studying the interplay between nonribosomal peptide synthetases (NRPS), a major source of secondary metabolites, and crucial external modifying enzymes is a challenging task since the interactions involved are often transient in nature. By applying a range of synthetic inhibitor-type compounds, a stabilized complex appropriate for structural analysis was generated for such a tailoring enzyme and an NRPS domain. The complex studied comprises an NRPS peptidyl carrier protein (PCP) domain bound to the Cytochrome P450 enzyme that is crucial for the provision of β-hydroxylated amino acid precursors in the biosynthesis of the cyclic depsipeptide skyllamycin. The structure reveals that complex formation is governed by hydrophobic interactions, the presence of which can be controlled through minor alterations in PCP structure that enable selectivity amongst multiple highly similar PCP domains.

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Language(s): eng - English
 Dates: 2014-05-052014-07-092014-08-04
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 7992
DOI: 10.1002/anie.201404977
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Title: Angewandte Chemie International Edition : a journal of the Gesellschaft Deutscher Chemiker
Source Genre: Journal
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Pages: - Volume / Issue: 53 (32) Sequence Number: - Start / End Page: 8518 - 8522 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/110984073528720