Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from Hevea Brasiliensis
作者： K. Gruber , M. Gugganig , U. G. Wagner , C. Kratky
DOI: 10.1515/BC.1999.123
关键词:
摘要: The X-ray crystal structure of native hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined to a final R 11.5% for all data and an Rfree 14.4%. favorable data-to-parameter ratio atomic resolution made the refinement individual anisotropic displacement parameters possible. also allowed clear distinction alternate orientations histidine majority asparagine glutamine side chains. number hydrogen atoms, including one on imidazole mechanistically important His-235, became visible as peaks in difference electron density map. revealed discretely disordered sidechain Ser-80, which is part putative catalytic triad. Analysis anisotropy indicated increased mobility residues near entrance active site within site.
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