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- Title
Crystallization and preliminary X-ray crystallographic analysis of a putative nonribosomal peptide synthase AmbB from Pseudomonas aeruginosa.
- Authors
Wang, Yiwen; Li, Dewang; Huan, Xuelu; Zhang, Lianhui; Song, Haiwei
- Abstract
AmbB is a putative nonribosomal peptide synthase from Pseudomonas aeruginosa, which is involved in the production of IQS, a potent cell-cell communication signal molecule that integrates the quorum-sensing mechanism and stress response. It consists of 1249 amino acids and contains an AMP-binding domain, a phosphopantetheine-binding (PB) domain and a condensation (C) domain. In this report, a truncated form of AmbB that contains the PB domain and the condensation domain was overexpressed with an N-terminal GST tag in Escherichia coli and purified as a monomer using affinity and size-exclusion chromatography. The recombinant AmbBc (comprising residues 727-1249 of full-length AmbB) was crystallized using the hanging-drop vapour-diffusion method and a full data set was collected to 2.45 Å resolution using a synchrotron-radiation source. The crystals belonged to space group P6122 or P6522, with unit-cell parameters a = b = 87.81, c = 286.8 Å, α = 90, β = 90, γ = 120°, and contained one molecule per asymmetric unit.
- Subjects
NONRIBOSOMAL peptide synthetases; PSEUDOMONAS aeruginosa; CELL communication; QUORUM sensing; PHOSPHOPANTETHEINE
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 3, p339
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14001782