Download MendeleyBrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative beta-lactamase-like protein from Brucella melitensis.
Abendroth, J., Sankaran, B., Edwards, T.E., Gardberg, A.S., Dieterich, S., Bhandari, J., Napuli, A.J., Van Voorhis, W.C., Staker, B.L., Myler, P.J., Stewart, L.J.(2011) Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 1106-1112
- PubMed: 21904058
- DOI: https://doi.org/10.1107/S1744309111010220
- Primary Citation of Related Structures:
3MD7, 3PY5, 3PY6, 3QH8 - PubMed 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.
Organizational Affiliation:
Seattle Structural Genomics Center for Infectious Disease (SSGCID), USA. jabendroth@embios.com
