Abstract
Crystals of pokeweed antiviral protein (PAP) from seeds of Phytolacca americana with high diffraction ability were grown from high protein concentration (100 mg/mL) solution at high temperature (33°C). The crystal structure was solved by use of molecular replacement method and refined by use of molecular dynamic method at 0-25 nm to an R factor of 18.15% with standard deviations from standard geometry of 0.001 6 nm and 2.04° for bond lengths and bond angles, respectively. Comparison with two other PAPs revealed, near the active center, a sequence-and structure-variable region, consisting of the loop connecting the fifth β-strand with the second α-helix and including a proposed active residue, suggesting this loop probably to be related to difference in activity.
Original language | English (US) |
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Pages (from-to) | 413-418 |
Number of pages | 6 |
Journal | Science in China, Series C: Life Sciences |
Volume | 41 |
Issue number | 4 |
DOIs | |
State | Published - 1998 |
Externally published | Yes |
Keywords
- Crystal structure
- Pokeweed antiviral protein
- Ribosome inactivating protein
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology
- General Environmental Science
- General Agricultural and Biological Sciences