1JCD

Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations

1JCD の概要

• エントリーDOI: 10.2210/pdb1jcd/pdb
• 関連するPDBエントリー: 1EQ7 1JCB 1JCC
• 分子名称: MAJOR OUTER MEMBRANE LIPOPROTEIN (2 entities in total)
• 機能のキーワード: lipoprotein, protein folding, coiled coil, helix capping, alanine-zipper, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane ; Lipid-anchor : P69776
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 15504.68

構造登録者

Liu, J.,Lu, M. (登録日: 2001-06-08, 公開日: 2003-06-17, 最終更新日: 2023-08-16)

主引用文献

Liu, J.,Lu, M.
An Alanine-Zipper Structure Determined by Long Range Intermolecular Interactions
J.Biol.Chem., 277:48708-48713, 2002

PubMed Abstract: A major challenge in protein folding is to identify and quantify specific structural determinants that allow native proteins to acquire their unique folded structures. Here we report the engineering of a 52-residue protein (Ala-14) that contains exclusively alanine residues at the hydrophobic a and d positions of a natural heptad-repeat sequence. Ala-14 is unfolded under normal solution conditions yet forms a parallel three-stranded alpha-helical coiled coil in crystals. Ala-14 trimers in the solid state associate with each other through the pairing of polar side chains and formation of an extended network of water-mediated hydrogen bonds. In contrast to the classical view that local intramolecular tertiary interactions dictate the three-dimensional structure of small single-domain proteins, Ala-14 shows that long range intermolecular interactions can be essential in determining the metastable alanine-zipper structure. A similar interplay between short range local and longer range global forces may underlie the conformational properties of the growing class of natively unstructured proteins in biological processes.

PubMed: 12368282
DOI: 10.1074/jbc.M208773200

実験手法

X-RAY DIFFRACTION (1.3 Å)