Mapping of the Communication-Mediating Interface in Nonribosomal Peptide Synthetases Using a Genetically Encoded Photocrosslinker Supports an Upside-Down Helix-Hand Motif
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- 作者：Eva Dehling&dagger ; ; Gerrit Volkmann&dagger ; ; Julian C.J. Matern ; Wolfgang Dö ; rner ; Jonas Alfermann ; Julia Diecker ; Henning D. Mootz ; henning.mootz@uni-muenster.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：BpF ; para-benzoyl-L-phenylalanine ; C domain ; condensation domain ; COM domain ; communication-mediating domain ; DKP ; diketopiperazine ; E domain ; epimerization domain ; GrsA ; gramicidin S synthetase 1 ; MALDI-TOF ; matrix-assisted laser desorption ionization ; MS ; mass spectrometry ; NRPS ; nonribosomal peptide synthetase ; PCP ; peptidyl carrier protein ; PKS ; polyketide synthase ; Ppant ; 4&prime ; -phosphopantetheine ; SBP ; streptavidin-binding peptide ; SrfA-C ; surfactin synthetase 3 ; TE ; thioesterase ; TOF ; t
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：23 October 2016
- 年：2016
- 卷：428
- 期：21
- 页码：4345-4360
- 全文大小：1804 K
文摘
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NRPS subunit interaction was studied with a photocrosslinking amino acid.
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Three hydrophobic residues in a C-terminal donor helix are key interaction points.
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Residues from the interior of the acceptor NRPS module are contacting the donor helix.
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Mapping of crosslinks reveals reversed helix orientation compared to a previous model.
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First direct insight into the architecture of interaction important for NRPS engineering