7X0E

Structure of Pseudomonas NRPS protein, AmbB-TC in apo form

7X0E の概要

• エントリーDOI: 10.2210/pdb7x0e/pdb
• 分子名称: AMB antimetabolite synthase AmbB, N-methyl-N-[(2S,3R,4R,5R)-2,3,4,5,6-pentakis(oxidanyl)hexyl]nonanamide (3 entities in total)
• 機能のキーワード: non-ribosomal peptide synthetase, ambb, pseudomonas, biosynthetic protein
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56306.09

構造登録者

ChuYuanKee, M.,Bharath, S.R.,Song, H. (登録日: 2022-02-22, 公開日: 2022-07-06, 最終更新日: 2024-05-29)

主引用文献

Chu Yuan Kee, M.J.,Bharath, S.R.,Wee, S.,Bowler, M.W.,Gunaratne, J.,Pan, S.,Zhang, L.,Song, H.
Structural insights into the substrate-bound condensation domains of non-ribosomal peptide synthetase AmbB.
Sci Rep, 12:5353-5353, 2022

PubMed Abstract: Non-ribosomal peptide synthetases (NRPS) are multi-modular/domain enzymes that catalyze the synthesis of bioactive peptides. A crucial step in the process is peptide elongation accomplished by the condensation (C) domain with the aid of a peptidyl carrier or thiolation (T) domain. Here, we examined condensation reaction carried out by NRPS AmbB involved in biosynthesis of L-2-amino-4-methoxy-trans-3-butenoic acid (AMB) in P. aeruginosa. We determined crystal structures of the truncated T-C bidomain of AmbB in three forms, the apo enzyme with disordered T domain, the holo form with serine linked phosphopantetheine (Ppant) and a holo form with substrate (L-alanine) loaded onto Ppant. The two holo forms feature the T domain in a substrate-donation conformation. Mutagenesis combined with functional assays identified residues essential for the attachment of Ppant, anchoring the Ppant-L-Ala in the donor catalytic channel and the role of the conserved His953 in condensation activity. Altogether, these results provide structural insights into the condensation reaction at the donor site with a substrate-bound C domain of AmbB and lay the foundation for understanding the molecular mechanism of condensation which is crucial for AMB synthesis.

PubMed: 35354859
DOI: 10.1038/s41598-022-09188-8

実験手法

X-RAY DIFFRACTION (2.1 Å)