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dc.contributor.authorLee, T. Verne
dc.contributor.authorJohnson, Linda J.
dc.contributor.authorJohnson, Richard D.
dc.contributor.authorKoulman, Albert
dc.contributor.authorLane, Geoffrey A.
dc.contributor.authorLott, J. Shaun
dc.contributor.authorArcus, Vickery L.
dc.coverage.spatialUnited Statesen_NZ
dc.date.accessioned2010-02-15T03:01:44Z
dc.date.available2010-02-15T03:01:44Z
dc.date.issued2010
dc.identifier.citationLee, T.V., Johnson, L.J., Johnson, R.D., Koulman, A., Lane, G.A., Lott, J.S. & Arcus, V.L. (2010). Structure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesis. Journal of Biological Chemistry, 285(4), 2415-2427.en
dc.identifier.issn0021-9258
dc.identifier.urihttps://hdl.handle.net/10289/3572
dc.description.abstractNonribosomal peptide synthetases (NRPSs) are large, multidomain proteins that are involved in the biosynthesis of an array of secondary metabolites. We report the structure of the third adenylation domain from the siderophore-synthesizing NRPS, SidN, from the endophytic fungus Neotyphodium lolii. This is the first structure of a eukaryotic NRPS domain, and it reveals a large binding pocket required to accommodate the unusual amino acid substrate, N-delta-cis-anhydromevalonyl-N-delta-hydroxy-L-ornithine (cis-AMHO). The specific activation of cis-AMHO was confirmed biochemically, and an AMHO moiety was unambiguously identified as a component of the fungal siderophore using mass spectroscopy. The protein structure shows that the substrate binding pocket is defined by 17 amino acid residues, in contrast to both prokaryotic adenylation domains and to previous predictions based on modeling. Existing substrate prediction methods for NRPS adenylation domains fail for domains from eukaryotes due to the divergence of their signature sequences from those of prokaryotes. Thus, this new structure will provide a basis for improving prediction methods for eukaryotic NRPS enzymes that play important and diverse roles in the biology of fungi.en
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherThe American Society for Biochemistry and Molecular Biologyen
dc.rightsThis research was originally published in the Journal of Biological Chemistry. Lee, T.V., Johnson, L.J., Johnson, R.D., Koulman, A., Lane, G.A., Lott, J.S. & Arcus, V.L. Structure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesis. Journal of Biological Chemistry. 2010. 285: 2415-2427. © the American Society for Biochemistry and Molecular Biology.en
dc.subjectacetyl-coa synthetaseen
dc.subjectcrystal-structureen
dc.subjectsubstrate-specificityen
dc.subjectaspergillus-nidulansen
dc.subjectdensity modificationen
dc.subjectfirefly luciferaseen
dc.subjectprotein-productionen
dc.subjectgramicidin-Sen
dc.subjectcoenzyme-Aen
dc.subjectbindingen
dc.titleStructure of a eukaryotic nonribosomal peptide synthetase adenylation domain that activates a large hydroxamate amino acid in siderophore biosynthesisen
dc.typeJournal Articleen
dc.identifier.doi10.1074/jbc.M109.071324en
dc.relation.isPartOfJournal of Biological Chemistryen_NZ
pubs.begin-page2415en_NZ
pubs.elements-id34665
pubs.end-page2427en_NZ
pubs.issue4en_NZ
pubs.volume285en_NZ


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