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12‐Bromododecanoic acid binds inside the calyx of bovine β‐lactoglobulin
Author(s) -
Qin Bin Y,
Creamer Lawrence K,
Baker Edward N,
Jameson Geoffrey B
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01199-5
Subject(s) - calyx , chemistry , ligand (biochemistry) , carboxylate , crystallization , crystallography , molecule , stereochemistry , receptor , biochemistry , organic chemistry , biology , botany
The X‐ray structure of bovine β‐lactoglobulin with the ligand 12‐bromododecanoic acid as a model for fatty acids has been determined at a resolution of 2.23 Å in the trigonal lattice Z form. The ligand binds inside the calyx, resolving a long‐standing controversy as to where fatty‐acid like ligands bind. The carboxylate head group lies at the surface of the molecule, and the lid to the calyx is open at the pH of crystallization (pH 7.3), consistent with the conformation observed in ligand‐free bovine β‐lactoglobulin in lattice Z at pH 7.1 and pH 8.2.