期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 125, 期 41, 页码 12475-12483出版社
AMER CHEMICAL SOC
DOI: 10.1021/JA036756q
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资金
- NCI NIH HHS [CA89810] Funding Source: Medline
- NCRR NIH HHS [RR00862] Funding Source: Medline
- NIGMS NIH HHS [GM59908, GM55843, GM61898, GM38660, GM64530] Funding Source: Medline
Microcin J25 (MccJ25) is a 21-amino acid peptide inhibitor active against the DNA-dependent RNA polymerase of Gram negative bacteria. Previously, the structure of MccJ25 was reported to be a head-to-tail circle, cyclo(-G(1)GAGHVPEYF(10)VGIGTPISFY(20)G-). On the basis of biochemical studies, mass spectrometry, and NMR, we show that this structure is incorrect, and that the peptide has an extraordinary structural fold. MccJ25 contains an internal lactam linkage between the alpha-amino group of Glyl and the gamma-carboxyl of Glu8. The tail (Tyr9-Gly21) passes through the ring (Gly1-Glu8), with Phe19 and Tyr20 straddling each side of the ring, sterically trapping the tail in a noncovalent interaction we call a lassoed tail.
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