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

DOI: 10.1107/S2053230X14007298 DOI Help
PMID: 24817726 PMID Help

Authors: Diana Vieira (Macromolecular Crystallography Group and GlycoLab, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa) , Teresa A. Figueiredo (Laboratory of Molecular Genetics, Microbiology of Human Pathogens Unit, Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa) , Anil Verma (Oxford Protein Production Facility, Research Complex at Harwell, Didcot, England) , Rita G. Sobral (Laboratory of Molecular Genetics, Microbiology of Human Pathogens Unit, Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa) , Ana M. Ludovice (Laboratory of Molecular Genetics, Microbiology of Human Pathogens Unit, Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa) , Hermínia De Lencastre (Laboratory of Molecular Genetics, Microbiology of Human Pathogens Unit, Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa) , Jose Trincao (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 632 - 635

State: Published (Approved)
Published: May 2014

Abstract: Amidation of peptidoglycan is an essential feature in Staphylococcus aureus that is necessary for resistance to [beta]-lactams and lysozyme. GatD, a 27 kDa 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 2.25 Å, 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.

Journal Keywords: Gatd; Glutamine Amidotransferase-Like Protein; Staphylococcus Aureus

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

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