STRUCTURE OF PIG PLASMA RETINOL-BINDING PROTEIN AT 1.65 ANGSTROM RESOLUTION

The crystal structure of pig plasma retinol-binding protein (REP) has been determined at 1.65 Angstrom resolution. The space group is P2(1)2 (1)2(1), with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) Angstrom and one protein molecule in the asymmetric unit. The structure has been s olved using the molecular replacement method and refined with restrain ed least squares to an R factor of 0.1844 and an R-free of 0.237 for 1 8 874 and 1001 independent reflections, respectively. The relatively h igh resolution structure of pig holoRBP has revealed some new structur al details. Moreover, it has provided a description of the binding sit e for Cd2+, a metal ion which is required for protein crystallization. The hepta-coordination of the REP-bound cadmium ion involves differen t residues of two symmetry-related REP molecules, consistent with the participation of the cation in intermolecular interactions that in tur n promote protein crystallization.