1QJ4

Atomic Resolution Crystal Structure of Hydroxynitrile Lyase from Hevea Brasiliensis

(1999) Biol Chem 380: 993

• PubMed: 10494852 Search on PubMed
• DOI: https://doi.org/10.1515/BC.1999.123
• Primary Citation of Related Structures:  
  1QJ4


• PubMed Abstract: 
  

  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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Organizational Affiliation: 

Abteilung für Strukturbiologie, Institut für Physikalische Chemie, Universität Graz, Austria.