2HY6
A seven-helix coiled coil
2HY6 の概要
| エントリーDOI | 10.2210/pdb2hy6/pdb |
| 関連するPDBエントリー | 1GCL 1GCM 2B1F 2B22 2ZTA |
| 分子名称 | General control protein GCN4, HEXANE-1,6-DIOL (3 entities in total) |
| 機能のキーワード | protein design, parallel heptamer, protein structure, biosynthetic protein |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Nucleus: P03069 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 26454.84 |
| 構造登録者 | Liu, J.,Zheng, Q.,Deng, Y.,Cheng, C.S.,Kallenbach, N.R.,Lu, M. (登録日: 2006-08-04, 公開日: 2006-10-24, 最終更新日: 2023-08-30) |
| 主引用文献 | Liu, J.,Zheng, Q.,Deng, Y.,Cheng, C.S.,Kallenbach, N.R.,Lu, M. A seven-helix coiled coil. Proc.Natl.Acad.Sci.Usa, 103:15457-15462, 2006 Cited by PubMed Abstract: Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the overall coiled-coil architecture, we replaced all eight e and g residues in the GCN4 leucine zipper with nonpolar alanine side chains. Surprisingly, the alanine-containing mutant forms a stable alpha-helical heptamer in aqueous solution. The 1.25-A resolution crystal structure of the heptamer reveals a parallel seven-stranded coiled coil enclosing a large tubular channel with an unusual heptad register shift between adjacent staggered helices. The overall geometry comprises two interleaved hydrophobic helical screws of interacting cross-sectional a and d layers that have not been seen before. Moreover, asparagines at the a positions play an essential role in heptamer formation by participating in a set of buried interhelix hydrogen bonds. These results demonstrate that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of alpha-helices. PubMed: 17030805DOI: 10.1073/pnas.0604871103 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.25 Å) |
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