1ave
From Proteopedia
CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES
Overview
The three-dimensional structure of hen egg-white apo-avidin, crystallized in a tetragonal crystal form, has been refined to a crystallographic R-factor of 0.164 (for the 6390 observed reflections in the 10.0 to 2.8 A resolution range). As in the case of holo-avidin, from which starting atomic co-ordinates were derived, the functional tetramer shows 2-pseudo 22 molecular symmetry. Each promoter is organized in an eight-stranded antiparallel orthogonal beta-barrel, with extended loop regions, which define the biotin binding pocket in the protomer core. In the absence of biotin the binding site is only partly occupied by water molecules. The structure of the binding site residues, as observed in apo-avidin, is highly complementary to that of the incoming biotin molecule, accounting for prompt and specific recognition. A crystal lattice contact may play a role in stabilizing the conformation of one protein loop, part of the biotin-binding pocket.
About this Structure
1AVE is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Crystal structure of apo-avidin from hen egg-white., Pugliese L, Malcovati M, Coda A, Bolognesi M, J Mol Biol. 1994 Jan 7;235(1):42-6. PMID:8289264 Page seeded by OCA on Fri May 2 10:44:22 2008
