Characterization of the mononickel metallocenter in H134A mutant urease
IS Park, LO Michel, MA Pearson, E Jabri… - Journal of Biological …, 1996 - ASBMB
A mutant form of Klebsiella aerogenes urease possessing Ala instead of His at position 134
(H134A) is inactive and binds approximately half the normal complement of nickel (Park, I.-
S., and Hausinger, RP (1993) Protein Sci. 2, 1034-1041). The crystal structure of the H134A
protein was obtained at 2.0-Å resolution, and it confirms that only Ni-1 of the two nickel ions
found in the native enzyme is present. In contrast to the pseudotetrahedral geometry
observed for Ni-1 in native urease (where it is liganded by His-246, His-272, one oxygen …
(H134A) is inactive and binds approximately half the normal complement of nickel (Park, I.-
S., and Hausinger, RP (1993) Protein Sci. 2, 1034-1041). The crystal structure of the H134A
protein was obtained at 2.0-Å resolution, and it confirms that only Ni-1 of the two nickel ions
found in the native enzyme is present. In contrast to the pseudotetrahedral geometry
observed for Ni-1 in native urease (where it is liganded by His-246, His-272, one oxygen …
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