The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain.
CHAPS [3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate] is a non-denaturing detergent widely used for protein solubilization and stabilization. CHAPS was used to avoid protein aggregation during concentration of the recombinant stromelysin-3 (ST3) catalytic domain and was required to stabilize the protein, allowing its crystallization. The crystal structure of the complex between the ST3 catalytic domain and a phosphinic inhibitor shows two CHAPS molecules binding to ST3 in two different orientations. One CHAPS molecule is masking a hydrophobic surface of the protein, thus avoiding protein aggregation. This detergent molecule is also involved in packing interactions. The other detergent molecule is located in a pocket formed by the N- and C-terminal parts of the ST3 and stabilizes a loop that normally binds a Ca atom.
Gall
Anne-Laure
AL
Institut de Génomique et de Biologie Moléculaire et Cellulaire, Département de Biologie et Génomique Structurales, 1 Rue Laurent Fries, BP 10142, 67404 Illkirch CEDEX, France.
Ruff
Marc
M
Moras
Dino
D
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D002793:Cholic Acids / Q000737:chemistry*; D003460:Crystallization; D003902:Detergents; D007202:Indicators and Reagents; D053507:Matrix Metalloproteinase 11; D008666:Metalloendopeptidases / Q000737:chemistry*; D008969:Molecular Sequence Data; D013499:Surface Properties
D002793:Cholic Acids; D003902:Detergents; D007202:Indicators and Reagents; D053507:Matrix Metalloproteinase 11; D008666:Metalloendopeptidases; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate