8QPY

Solution NMR structure of the peptidyl carrier domain TomAPCP from the Tomaymycin non-ribosomal peptide synthetase

8QPY の概要

• エントリーDOI: 10.2210/pdb8qpy/pdb
• NMR情報: BMRB: 34868
• 分子名称: Carrier protein TomAPCP (1 entity in total)
• 機能のキーワード: non-ribosomal peptide synthetase, tomaymycin, pcp, phosphopantetheine, donor, biosynthetic protein
• 由来する生物種: Streptomyces regensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10380.38

構造登録者

Karanth, M.N.,Kirkpatrick, J.P.,Carlomagno, T. (登録日: 2023-10-03, 公開日: 2024-06-26, 最終更新日: 2024-07-03)

主引用文献

Karanth, M.N.,Kirkpatrick, J.P.,Krausze, J.,Schmelz, S.,Scrima, A.,Carlomagno, T.
The specificity of intermodular recognition in a prototypical nonribosomal peptide synthetase depends on an adaptor domain.
Sci Adv, 10:eadm9404-eadm9404, 2024

PubMed Abstract: In the quest for new bioactive substances, nonribosomal peptide synthetases (NRPS) provide biodiversity by synthesizing nonproteinaceous peptides with high cellular activity. NRPS machinery consists of multiple modules, each catalyzing a unique series of chemical reactions. Incomplete understanding of the biophysical principles orchestrating these reaction arrays limits the exploitation of NRPSs in synthetic biology. Here, we use nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry to solve the conundrum of how intermodular recognition is coupled with loaded carrier protein specificity in the tomaymycin NRPS. We discover an adaptor domain that directly recruits the loaded carrier protein from the initiation module to the elongation module and reveal its mechanism of action. The adaptor domain of the type found here has specificity rules that could potentially be exploited in the design of engineered NRPS machinery.

PubMed: 38896613
DOI: 10.1126/sciadv.adm9404

実験手法

SOLUTION NMR