2O6N

RH4B: designed right-handed coiled coil tetramer with all biological amino acids

2O6N の概要

• エントリーDOI: 10.2210/pdb2o6n/pdb
• 関連するPDBエントリー: 1RH4 1TGG
• 分子名称: RH4B designed peptide, YTTERBIUM (II) ION (3 entities in total)
• 機能のキーワード: right-handed, tetramer, de novo protein
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4120.63

構造登録者

Sales, M.,Alber, T. (登録日: 2006-12-07, 公開日: 2007-10-23, 最終更新日: 2023-12-27)

主引用文献

Sales, M.,Plecs, J.J.,Holton, J.M.,Alber, T.
Structure of a designed, right-handed coiled-coil tetramer containing all biological amino acids.
Protein Sci., 16:2224-2232, 2007

PubMed Abstract: The previous design of an unprecedented family of two-, three-, and four-helical, right-handed coiled coils utilized nonbiological amino acids to efficiently pack spaces in the oligomer cores. Here we show that a stable, right-handed parallel tetrameric coiled coil, called RH4B, can be designed entirely using biological amino acids. The X-ray crystal structure of RH4B was determined to 1.1 Angstrom resolution using a designed metal binding site to coordinate a single Yb(2+) ion per 33-amino acid polypeptide chain. The resulting experimental phases were particularly accurate, and the experimental electron density map provided an especially clear, unbiased view of the molecule. The RH4B structure closely matched the design, with equivalent core rotamers and an overall root-mean-square deviation for the N-terminal repeat of the tetramer of 0.24 Angstrom. The clarity and resolution of the electron density map, however, revealed alternate rotamers and structural differences between the three sequence repeats in the molecule. These results suggest that the RH4B structure populates an unanticipated variety of structures.

PubMed: 17766380
DOI: 10.1110/ps.062702907

実験手法

X-RAY DIFFRACTION (1.1 Å)