Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs+-selective binding site

Arai, S.; Yonezawa, Y.; Okazaki, N.; Matsumoto, F.; Shibazaki, C.; Shimizu, R.; Yamada, M.; Adachi, M.; Tamada, T.; Kawamoto, M.; Tokunaga, H.; Ishibashi, M.; Blaber, M.; Tokunaga, M.; Kuroki, R.

doi:10.1107/S1399004714027734

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

IUCr IT WDC

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Figure 3
Relaxed stereoview of the catalytic residues (grey sticks) and hydrophobic cluster (green sticks) of WT-HaBLA. The structure of EaBLA (blue) is superposed based on the catalytic residues (Ser65, Lys68, Tyr151, Glu273 and Lys316 of HaBLA). The side chains are omitted apart from those of the residues of the catalytic site and the hydrophobic cluster.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 3| February 2015| Pages 541-554

doi:10.1107/S1399004714027734

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