Purification, crystallization and preliminary X-ray diffraction analysis of GatD, a glutamine amidotransferase-like protein from Staphylococcus aureus peptidoglycan

Diana Vieira, Teresa A. Figueiredo, Anil Verma, Rita G. Sobral, Ana M. Ludovice, H. de Lencastre, Jose Trincao

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Amidation of peptidoglycan is an essential feature in Staphylococcus aureus that is necessary for resistance to β-lactams and lysozyme. GatD, a 27kDa type I glutamine amidotransferase-like protein, together with MurT ligase, catalyses the amidation reaction of the glutamic acid residues of the peptidoglycan of S. aureus. The native and the selenomethionine-derivative proteins were crystallized using the sitting-drop vapour-diffusion method with polyethylene glycol, sodium acetate and calcium acetate. The crystals obtained diffracted beyond 1.85 and 2.25Å, respectively, and belonged to space group P212121. X-ray diffraction data sets were collected at Diamond Light Source (on beamlines I02 and I04) and were used to obtain initial phases.

Original languageEnglish
Pages (from-to)632-635
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue numberPart 5
DOIs
Publication statusPublished - May 2014

Keywords

  • GatD
  • glutamine amidotransferase-like protein
  • Staphylococcus aureus

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