A novel 8-nm protein cage formed by Vibrio cholerae acylphosphatase
作者： Seema Nath , Ramanuj Banerjee , Udayaditya Sen , None
DOI: 10.1016/J.JMB.2013.09.014
关键词: Crystallography 、 Protein crystallization 、 Protein cage 、 Enzyme 、 Crystal structure 、 Stereochemistry 、 Chemistry 、 Cage 、 Trimer 、 Vibrio cholerae 、 Acylphosphatase
摘要: Here we show the formation of an ~8-nm cage formed by self-assembly acylphosphatase from Vibrio cholerae O395 (Vc-AcP). The 12-subunit structure forms spontaneously and is stabilized through binding sulfate ions at its exterior face interfacial regions. Crystal studies in solutions illuminate basis for cage, while a single (Cys20→Arg) mutation (Vc-AcP-C20R) transforms Vc-AcP to potent enzyme but disrupts assembly into trimer.
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