| Autor: |
K, Gruber, M, Gugganig, U G, Wagner, C, Kratky |
| Rok vydání: |
1999 |
| Předmět: |
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| Zdroj: |
Biological chemistry. 380(7-8) |
| ISSN: |
1431-6730 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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