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Title
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Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis.
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Authors
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K.Gruber,
M.Gugganig,
U.G.Wagner,
C.Kratky.
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Ref.
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Biol Chem, 1999,
380,
993-1000.
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PubMed id
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Abstract
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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 of 11.5% for all data and an Rfree of 14.4%. The favorable
data-to-parameter ratio at atomic resolution made the refinement of individual
anisotropic displacement parameters possible. The data also allowed a clear
distinction of the alternate orientations of all histidine and the majority of
asparagine and glutamine side chains. A number of hydrogen atoms, including one
on the imidazole of the mechanistically important His-235, became visible as
peaks in a difference electron density map. The structure revealed a discretely
disordered sidechain of Ser-80, which is part of the putative catalytic triad.
Analysis of the anisotropy indicated an increased mobility of residues near the
entrance to the active site and within the active site.
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