期刊
ACS CHEMICAL BIOLOGY
卷 11, 期 9, 页码 2466-2474出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.6b00345
关键词
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资金
- National Institutes of Health [GM106112]
- Welch Foundation [F-1712]
- College of Natural Sciences
- Office of the Executive Vice President and Provost
- Institute for Cellular and Molecular Biology
- National Institutes of Health, National Institute of General Medical Sciences
- Howard Hughes Medical Institute
- Office of Science, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-AC02- 05CH11231]
The polypeptides of multimodular polyketide synthases self-assemble into biosynthetic factories. While the docking domains that mediate the assembly of cis-acyltransferase polyketide synthase polypeptides are well-studied, those of the more recently discovered trans-acyltransferase polyketide synthases have just started to be described. Located at the C- and N-termini of many polypeptides, these 25-residue, two-helix, pseudosymmetric motifs noncovalently connect domains both between and within modules. Domains expressed with their natural, cognate docking motifs formed complexes stable to size-exclusion chromatography with 1-10 mu M dissociation constants as measured by isothermal titration calorimetry. Deletion and swapping experiments demonstrate portability of the docking motifs. A 1.72 angstrom-resolution structure of the N-terminal portion of the macrolactin synthase polypeptide MlnE shows an uncomplexed N-terminal docking motif to be preorganized in the conformation it assumes within the docking domain complex.
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