title: BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a 'putative β-lactamase-like protein' from Brucella melitensis.
abstract: The crystal structure of a β-lactamase-like protein from Brucella melitensis was initially solved by SAD phasing from an in-house data set collected on a crystal soaked with iodide. A high-resolution data set was collected at a synchroton at the Se edge wavelength, which also provided an independent source of phasing using a small anomalous signal from metal ions in the active site. Comparisons of anomalous peak heights at various wavelengths allowed the identification of the active-site metal ions as manganese. In the native data set a partially occupied GMP could be identified. When co-crystallized with AMPPNP or GMPPNP, clear density for the hydrolyzed analogs was observed, providing hints to the function of the protein.
authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID), USA. jabendroth@embios.com
authors: Jan
authors: J
authors: Abendroth
authors: Banumathi
authors: B
authors: Sankaran
authors: Thomas E
authors: TE
authors: Edwards
authors: Anna S
authors: AS
authors: Gardberg
authors: Shellie
authors: S
authors: Dieterich
authors: Janhavi
authors: J
authors: Bhandari
authors: Alberto J
authors: AJ
authors: Napuli
authors: Wesley C
authors: WC
authors: Van Voorhis
authors: Bart L
authors: BL
authors: Staker
authors: Peter J
authors: PJ
authors: Myler
authors: Lance J
authors: LJ
authors: Stewart
mesh_terms: D017347:Brucella melitensis / Q000201:enzymology*; D018360:Crystallography, X-Ray; D008024:Ligands; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D040681:Structural Homology, Protein; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D008024:Ligands; D001618:beta-Lactamases