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

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dc.citation.firstpage1210en_US
dc.citation.issueNumber7en_US
dc.citation.journalTitleProteinsen_US
dc.citation.lastpage1218en_US
dc.citation.volumeNumber82en_US
dc.contributor.authorLohman, Jeremy R.en_US
dc.contributor.authorMa, Mingen_US
dc.contributor.authorCuff, Marianne E.en_US
dc.contributor.authorBigelow, Lanceen_US
dc.contributor.authorBearden, Jessicaen_US
dc.contributor.authorBabnigg, Gyorgyen_US
dc.contributor.authorJoachimiak, Andrzejen_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.contributor.authorShen, Benen_US
dc.date.accessioned2017-08-04T12:29:41Zen_US
dc.date.available2017-08-04T12:29:41Zen_US
dc.date.issued2014en_US
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.en_US
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.en_US
dc.identifier.digitalcrystal_structure_BlmIen_US
dc.identifier.doihttps://doi.org/10.1002/prot.24485en_US
dc.identifier.urihttps://hdl.handle.net/1911/96577en_US
dc.language.isoengen_US
dc.publisherWileyen_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Wiley.en_US
dc.titleThe crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteinsen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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