Crystallization (Comment) | Organism |
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structures of native monomeric, active dimeric, and diisopropyl fluorophosphate-inhibited dimeric protease, to respective resolutions of 2.05, 2.10 and 2.03 A. In the dimeric form, a functional oxyanion hole is formed by a loop of 10 aminoacid residues encompassing two consecutive arginine residues (Arg136 and Arg137). In the monomeric form, the top of the loop is shifted by approximately 11 A, resulting in a complete disruption of the oxyanion hole and loss of activity. The dimerization-induced allosteric changes are basis for the concentration-dependent activation of the protease | Suid alphaherpesvirus 1 |
Organism | UniProt | Comment | Textmining |
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Suid alphaherpesvirus 1 | Q83417 | - |
- |
Suid alphaherpesvirus 1 Kaplan | Q83417 | - |
- |
Subunits | Comment | Organism |
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More | concentration-dependent equilibrium of monomeric and dimeric protease in solution, small-angle X-ray scattering | Suid alphaherpesvirus 1 |
Synonyms | Comment | Organism |
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capsid scaffolding protein | - |
Suid alphaherpesvirus 1 |