The crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins

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dc.citation.firstpage1210
dc.citation.issueNumber7
dc.citation.journalTitleProteins
dc.citation.lastpage1218
dc.citation.volumeNumber82
dc.contributor.authorLohman, Jeremy R.
dc.contributor.authorMa, Ming
dc.contributor.authorCuff, Marianne E.
dc.contributor.authorBigelow, Lance
dc.contributor.authorBearden, Jessica
dc.contributor.authorBabnigg, Gyorgy
dc.contributor.authorJoachimiak, Andrzej
dc.contributor.authorPhillips, George N.Jr.
dc.contributor.authorShen, Ben
dc.date.accessioned2017-08-04T12:29:41Z
dc.date.available2017-08-04T12:29:41Z
dc.date.issued2014
dc.description.abstractCarrier proteins (CPs) play a critical role in the biosynthesis of various natural products, especially in nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) enzymology, where the CPs are referred to as peptidyl-carrier proteins (PCPs) or acyl-carrier proteins (ACPs), respectively. CPs can either be a domain in large multifunctional polypeptides or standalone proteins, termed Type I and Type II, respectively. There have been many biochemical studies of the Type I PKS and NRPS CPs, and of Type II ACPs. However, recently a number of Type II PCPs have been found and biochemically characterized. In order to understand the possible interaction surfaces for combinatorial biosynthetic efforts we crystallized the first characterized and representative Type II PCP member, BlmI, from the bleomycin biosynthetic pathway from Streptomyces verticillus ATCC 15003. The structure is similar to CPs in general but most closely resembles PCPs. Comparisons with previously determined PCP structures in complex with catalytic domains reveals a common interaction surface. This surface is highly variable in charge and shape, which likely confers specificity for interactions. Previous nuclear magnetic resonance (NMR) analysis of a prototypical Type I PCP excised from the multimodular context revealed three conformational states. Comparison of the states with the structure of BlmI and other PCPs reveals that only one of the NMR states is found in other studies, suggesting the other two states may not be relevant. The state represented by the BlmI crystal structure can therefore serve as a model for both Type I and Type II PCPs.
dc.identifier.citationLohman, Jeremy R., Ma, Ming, Cuff, Marianne E., et al.. "The crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins." <i>Proteins,</i> 82, no. 7 (2014) Wiley: 1210-1218. https://doi.org/10.1002/prot.24485.
dc.identifier.digitalcrystal_structure_BlmI
dc.identifier.doihttps://doi.org/10.1002/prot.24485
dc.identifier.urihttps://hdl.handle.net/1911/96577
dc.language.isoeng
dc.publisherWiley
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Wiley.
dc.titleThe crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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