[HTML][HTML] X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
TJ Fiedler, CA Davey, RE Fenna - Journal of Biological Chemistry, 2000 - ASBMB
The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 Å
resolution, using x-ray data recorded at− 180° C (r= 0.197, freer= 0.239). Results confirm
that the heme is covalently attached to the protein via two ester linkages between the
carboxyl groups of Glu 242 and Asp 94 and modified methyl groups on pyrrole rings A and C
of the heme as well as a sulfonium ion linkage between the sulfur atom of Met 243 and the β-
carbon of the vinyl group on pyrrole ring A. In the native enzyme a bound chloride ion has …
resolution, using x-ray data recorded at− 180° C (r= 0.197, freer= 0.239). Results confirm
that the heme is covalently attached to the protein via two ester linkages between the
carboxyl groups of Glu 242 and Asp 94 and modified methyl groups on pyrrole rings A and C
of the heme as well as a sulfonium ion linkage between the sulfur atom of Met 243 and the β-
carbon of the vinyl group on pyrrole ring A. In the native enzyme a bound chloride ion has …