1AVE

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

1AVE の概要

• エントリーDOI: 10.2210/pdb1ave/pdb
• 分子名称: AVIDIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: biotin-binding protein
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P02701
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29142.58

構造登録者

Pugliese, L.,Coda, A.,Malcovati, M.,Bolognesi, M. (登録日: 1993-03-05, 公開日: 1994-01-31, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)