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Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from <I>Hevea brasiliensis</I>
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K. Gruber
Published/Copyright:
June 1, 2005
Abstract
The X-ray crystal structure of native hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) has been determined at 1.1 Å 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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Published Online: 2005-06-01
Published in Print: 1999-07-01
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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