1AVE

CRYSTAL STRUCTURE OF HEN EGG-WHITE APO-AVIDIN IN RELATION TO ITS THERMAL STABILITY PROPERTIES

Summary for 1AVE

• Entry DOI: 10.2210/pdb1ave/pdb
• Descriptor: AVIDIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: biotin-binding protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P02701
• Total number of polymer chains: 2
• Total formula weight: 29142.58

Authors

Pugliese, L.,Coda, A.,Malcovati, M.,Bolognesi, M. (deposition date: 1993-03-05, release date: 1994-01-31, Last modification date: 2024-11-20)

Primary citation

Pugliese, L.,Malcovati, M.,Coda, A.,Bolognesi, M.
Crystal structure of apo-avidin from hen egg-white.
J.Mol.Biol., 235:42-46, 1994

PubMed Abstract: 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.

PubMed: 8289264

Experimental method

X-RAY DIFFRACTION (2.8 Å)