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

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.

doi:10.1107/S1744309111010220

Acta Crystallographica Section F
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Figure 4
AMP-bound and GMP-bound structures. BrabA.11339.a was cocrystallized with AMPPNP and GMPPNP, variants of AMP or GMP that are nonhydrolyzable between the β-phosphate and γ-phosphate. Left panels, OMIT densities for the AMPPNP (top) and GMPPNP (bottom) cocrystals (see Fig. 3

for colors). The σ_A-weighted 2F_o − F_c electron density for the high-resolution data set is contoured at 1σ (blue) and the corresponding F_o − F_c electron density is contoured at ±3σ (green/red). The right panels show the refined densities for the models refined with AMP (top) and GMP (bottom), respectively. No density is visible beyond the α-phosphate. It is likely that BrabA.11339.a has hydrolyzed the β-phosphate. The nucleotides are bound in the dimer interface and engage in multiple interactions with both protomers.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1106-1112

doi:10.1107/S1744309111010220

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