6EWU

Solution Structure of Rhabdopeptide NRPS Docking Domain Kj12C-NDD

6EWU の概要

• エントリーDOI: 10.2210/pdb6ewu/pdb
• NMR情報: BMRB: 34195
• 分子名称: NRPS Kj12C-NDD (1 entity in total)
• 機能のキーワード: protein, peptide binding protein
• 由来する生物種: Xenorhabdus stockiae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7322.09

構造登録者

Hacker, C.,Cai, X.,Kegler, C.,Zhao, L.,Weickhmann, A.K.,Bode, H.B.,Woehnert, J. (登録日: 2017-11-06, 公開日: 2018-10-31, 最終更新日: 2024-06-19)

主引用文献

Hacker, C.,Cai, X.,Kegler, C.,Zhao, L.,Weickhmann, A.K.,Wurm, J.P.,Bode, H.B.,Wohnert, J.
Structure-based redesign of docking domain interactions modulates the product spectrum of a rhabdopeptide-synthesizing NRPS.
Nat Commun, 9:4366-4366, 2018

PubMed Abstract: Several peptides in clinical use are derived from non-ribosomal peptide synthetases (NRPS). In these systems multiple NRPS subunits interact with each other in a specific linear order mediated by specific docking domains (DDs), whose structures are not known yet, to synthesize well-defined peptide products. In contrast to classical NRPSs, single-module NRPS subunits responsible for the generation of rhabdopeptide/xenortide-like peptides (RXPs) can act in different order depending on subunit stoichiometry thereby producing peptide libraries. To define the basis for their unusual interaction patterns, we determine the structures of all N-terminal DDs (DDs) as well as of an DD-DD complex and characterize all putative DD interactions thermodynamically for such a system. Key amino acid residues for DD interactions are identified that upon their exchange change the DD affinity and result in predictable changes in peptide production. Recognition rules for DD interactions are identified that also operate in other megasynthase complexes.

PubMed: 30341296
DOI: 10.1038/s41467-018-06712-1

実験手法

SOLID-STATE NMR