7TZ4

Salicylate Adenylate PchD from Pseudomonas aeruginosa containing 4-cyanosalicyl-AMS

7TZ4 の概要

• エントリーDOI: 10.2210/pdb7tz4/pdb
• 分子名称: Pyochelin biosynthesis salicyl-AMP ligase PchD, 5'-O-[(4-cyano-2-hydroxybenzoyl)sulfamoyl]adenosine (3 entities in total)
• 機能のキーワード: adenylate syntase, salicylate, biosynthetic protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60473.77

構造登録者

Shelton, C.L.,Meneely, K.M.,Lamb, A.L. (登録日: 2022-02-15, 公開日: 2022-05-18, 最終更新日: 2023-10-18)

主引用文献

Shelton, C.L.,Meneely, K.M.,Ronnebaum, T.A.,Chilton, A.S.,Riley, A.P.,Prisinzano, T.E.,Lamb, A.L.
Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD.
J.Biol.Inorg.Chem., 27:541-551, 2022

PubMed Abstract: Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5'-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii.

PubMed: 35513576
DOI: 10.1007/s00775-022-01941-8

実験手法

X-RAY DIFFRACTION (1.69 Å)