These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Crystallization and preliminary X-ray crystallographic analysis of a putative nonribosomal peptide synthase AmbB from Pseudomonas aeruginosa.
    Author: Wang Y, Li D, Huan X, Zhang L, Song H.
    Journal: Acta Crystallogr F Struct Biol Commun; 2014 Mar; 70(Pt 3):339-42. PubMed ID: 24598922.
    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.
    [Abstract] [Full Text] [Related] [New Search]