2JUG

Multienzyme Docking in Hybrid Megasynthetases

2JUG の概要

• エントリーDOI: 10.2210/pdb2jug/pdb
• NMR情報: BMRB: 15442
• 分子名称: TubC protein (1 entity in total)
• 機能のキーワード: docking domain, dimer, nonribosomal peptide synthetase, tubulysin, ligase, phosphopantetheine, biosynthetic protein
• 由来する生物種: Angiococcus disciformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16252.74

構造登録者

Richter, C.D.,Nietlispach, D.,Broadhurst, R.W.,Weissman, K.J. (登録日: 2007-08-24, 公開日: 2007-12-11, 最終更新日: 2024-05-29)

主引用文献

Richter, C.D.,Nietlispach, D.,Broadhurst, R.W.,Weissman, K.J.
Multienzyme docking in hybrid megasynthetases
Nat.Chem.Biol., 4:75-81, 2008

PubMed Abstract: Hybrid multienzyme systems composed of polyketide synthase (PKS) and nonribosomal polypeptide synthetase (NRPS) modules direct the biosynthesis of clinically valuable natural products in bacteria. The fidelity of this process depends on specific recognition between successive polypeptides in each assembly line-interactions that are mediated by terminal 'docking domains'. We have identified a new family of N-terminal docking domains, exemplified by TubCdd from the tubulysin system of Angiococcus disciformis An d48. TubCdd is homodimeric, which suggests that NRPS subunits in mixed systems self-associate to interact with partner PKS homodimers. The NMR structure of TubCdd reveals a new fold featuring an exposed beta-hairpin that serves as the binding site for the C-terminal docking domain of the partner polypeptide. The pattern of charged residues on the contact surface of the beta-hairpin is a key determinant of the interaction and seems to constitute a 'docking code' that can be used to alter binding affinity.

PubMed: 18066054
DOI: 10.1038/nchembio.2007.61

実験手法

SOLUTION NMR