6OM4

The structure of Microcin C7 biosynthetic enzyme MccB in complex with N-formylated MccA

6OM4 の概要

• エントリーDOI: 10.2210/pdb6om4/pdb
• 分子名称: MccB protein, Microcin C7, ZINC ION, ... (7 entities in total)
• 機能のキーワード: microcin c7, phosphoramidate, trojan horse antibiotic, biosynthetic protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 80564.36

構造登録者

Dong, S.-H.,Nair, S.K. (登録日: 2019-04-18, 公開日: 2019-05-22, 最終更新日: 2024-10-23)

主引用文献

Dong, S.H.,Kulikovsky, A.,Zukher, I.,Estrada, P.,Dubiley, S.,Severinov, K.,Nair, S.K.
Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by theN-formyl of the peptide precursor.
Chem Sci, 10:2391-2395, 2019

PubMed Abstract: Microcin C7 (McC) is a peptide antibiotic modified by a linkage of the terminal isoAsn amide to AMP a phosphoramidate bond. Post-translational modification on this ribosomally produced heptapeptide precursor is carried out by MccB, which consumes two equivalents of ATP to generate the N-P linkage. We demonstrate that MccB only efficiently processes the precursor heptapeptide that retains the -formylated initiator Met (fMet). Binding studies and kinetic measurements evidence the role of the -formyl moiety. Structural data show that the -formyl peptide binding results in an ordering of residues in the MccB "crossover loop", which dictates specificity in homologous ubiquitin activating enzymes. The -formyl peptide exhibits substrate inhibition, and cannot be displaced from MccB by the desformyl counterpart. Such substrate inhibition may be a strategy to avert unwanted McC buildup and avert toxicity in the cytoplasm of producing organisms.

PubMed: 30881667
DOI: 10.1039/c8sc03173h

実験手法

X-RAY DIFFRACTION (1.7 Å)