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Literature summary for 3.4.21.97 extracted from

  • Zuehlsdorf, M.; Werten, S.; Klupp, B.G.; Palm, G.J.; Mettenleiter, T.C.; Hinrichs, W.
    Dimerization-induced allosteric changes of the oxyanion-hole loop activate the pseudorabies virus assemblin pUL26N, a herpesvirus serine protease (2015), PLoS Pathog., 11, e1005045 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Suid alphaherpesvirus 1 Q83417
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Suid alphaherpesvirus 1 Kaplan Q83417
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Subunits

Subunits Comment Organism
More concentration-dependent equilibrium of monomeric and dimeric protease in solution, small-angle X-ray scattering Suid alphaherpesvirus 1

Synonyms

Synonyms Comment Organism
capsid scaffolding protein
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Suid alphaherpesvirus 1