2AVI
THREE-DIMENSIONAL STRUCTURES OF AVIDIN AND THE AVIDIN-BIOTIN COMPLEX
2AVI の概要
| エントリーDOI | 10.2210/pdb2avi/pdb |
| 分子名称 | AVIDIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, BIOTIN, ... (4 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 | 29631.20 |
| 構造登録者 | |
| 主引用文献 | Livnah, O.,Bayer, E.A.,Wilchek, M.,Sussman, J.L. Three-dimensional structures of avidin and the avidin-biotin complex. Proc.Natl.Acad.Sci.USA, 90:5076-5080, 1993 Cited by PubMed Abstract: The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each monomer is an eight-stranded antiparallel beta-barrel, remarkably similar to that of the genetically distinct bacterial analog streptavidin. As in streptavidin, binding of biotin involves a highly stabilized network of polar and hydrophobic interactions. There are, however, some differences. The presence of additional hydrophobic and hydrophilic groups in the binding site of avidin (which are missing in streptavidin) may account for its higher affinity constant. Two amino acid substitutions are proposed to be responsible for its susceptibility to denaturation relative to streptavidin. Unexpectedly, a residual N-acetylglucosamine moiety was detected in the deglycosylated avidin monomer by difference Fourier synthesis. PubMed: 8506353DOI: 10.1073/pnas.90.11.5076 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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