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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.
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. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Abendroth, J, Sankaran, B, Edwards, TE, Gardberg, AS, Dieterich, S, Bhandari, J, Napuli, AJ, Van Voorhis, WC, Staker, BL, Myler, PJ, Stewart, LJ |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 67 |
Issue | Pt 9 |
Pagination | 1106-12 |
Date Published | 2011 Sep 1 |
ISSN | 1744-3091 |
Keywords | beta-Lactamases, Brucella melitensis, Crystallography, X-Ray, Ligands, Models, Molecular, Protein Structure, Quaternary, Structural Homology, Protein |
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. |
DOI | 10.1107/S1744309111010220 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 21904058 |