6MFX

Crystal structure of a 4-domain construct of a mutant of LgrA in the substrate donation state

6MFX の概要

• エントリーDOI: 10.2210/pdb6mfx/pdb
• 分子名称: Linear gramicidin synthase subunit A, N-[2-(acetylamino)ethyl]-N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alaninamide, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, ... (5 entities in total)
• 機能のキーワード: nonribosomal peptide synthetase, tailoring domain, nrps, enzyme, natural product, linear gramicidin, ligase
• 由来する生物種: Brevibacillus parabrevis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 138960.85

構造登録者

Reimer, J.M.,Eivaskhani, M.,Schmeing, T.M. (登録日: 2018-09-12, 公開日: 2019-11-20, 最終更新日: 2024-10-30)

主引用文献

Reimer, J.M.,Eivaskhani, M.,Harb, I.,Guarne, A.,Weigt, M.,Schmeing, T.M.
Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility.
Science, 366:-, 2019

PubMed Abstract: Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes that synthesize natural product therapeutics using a modular synthetic logic, whereby each module adds one aminoacyl substrate to the nascent peptide. We have determined five x-ray crystal structures of large constructs of the NRPS linear gramicidin synthetase, including a structure of a full core dimodule in conformations organized for the condensation reaction and intermodular peptidyl substrate delivery. The structures reveal differences in the relative positions of adjacent modules, which are not strictly coupled to the catalytic cycle and are consistent with small-angle x-ray scattering data. The structures and covariation analysis of homologs allowed us to create mutants that improve the yield of a peptide from a module-swapped dimodular NRPS.

PubMed: 31699907
DOI: 10.1126/science.aaw4388

実験手法

X-RAY DIFFRACTION (2.2 Å)