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 2
Fold comparison. Comparison of the fold of BrabA.11339.a with its structural homologues. 3g1p is the PhnP protein from E. coli, 1zkp is a putative ribonuclease from B. anthracis and 1y44 is ribonuclease Z from B. subtilis. The structural homology is focused around the two β-sheets and helices α4 and α5. Color scheme: Mn, magenta; Zn, cyan; Na, green; K, blue

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309111010220

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