A novel 8-nm protein cage formed by Vibrio cholerae acylphosphatase.
Here we show the formation of an ~8-nm cage formed by the self-assembly of acylphosphatase from Vibrio cholerae O395 (Vc-AcP). The 12-subunit cage structure forms spontaneously and is stabilized through binding of sulfate ions at its exterior face and interfacial regions. Crystal structure and studies in solutions illuminate the basis for the formation of the cage, while a single (Cys20→Arg) mutation (Vc-AcP-C20R) transforms Vc-AcP to a potent enzyme but disrupts the assembly into a trimer.
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF, Bidhannagar, Kolkata 700064, India.
Seema
S
Nath
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF, Bidhannagar, Kolkata 700064, India.
Ramanuj
R
Banerjee
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF, Bidhannagar, Kolkata 700064, India. Electronic address: udayaditya.sen@saha.ac.in.
Udayaditya
U
Sen
D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D019943:Amino Acid Substitution; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D055503:Protein Multimerization; D014734:Vibrio cholerae / Q000201:enzymology*; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D050505:Mutant Proteins; D000097024:Acylphosphatase
LT; X-ray crystallography; bacterial protein phosphatases; dynamic light scattering; loop mediated tetramer; protein crystallization; protein self-assembly