2FCS

X-ray Crystal Structure of a Chemically Synthesized [L-Gln35]Ubiquitin with a Cubic Space Group

2FCS の概要

• エントリーDOI: 10.2210/pdb2fcs/pdb
• 関連するPDBエントリー: 1YIW 1YJ1 2FCM 2FCN 2FCQ
• 分子名称: Ubiquitin, CADMIUM ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: ubiquitin, structural protein
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18319.81

構造登録者

Bang, D.,Gribenko, A.V.,Tereshko, V.,Kossiakoff, A.A.,Kent, S.B.,Makhatadze, G.I. (登録日: 2005-12-12, 公開日: 2006-01-31, 最終更新日: 2023-08-30)

主引用文献

Bang, D.,Gribenko, A.V.,Tereshko, V.,Kossiakoff, A.A.,Kent, S.B.,Makhatadze, G.I.
Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis.
Nat.Chem.Biol., 2:139-143, 2006

PubMed Abstract: The alpha-helix is a fundamental protein structural motif and is frequently terminated by a glycine residue. Explanations for the predominance of glycine at the C-cap terminal portions of alpha-helices have invoked uniquely favorable energetics of this residue in a left-handed conformation or enhanced solvation of the peptide backbone because of the absence of a side chain. Attempts to quantify the contributions of these two effects have been made previously, but the issue remains unresolved. Here we have used chemical protein synthesis to dissect the energetic basis of alpha-helix termination by comparing a series of ubiquitin variants containing an L-amino acid or the corresponding D-amino acid at the C-cap Gly35 position. D-Amino acids can adopt a left-handed conformation without energetic penalty, so the contributions of conformational strain and backbone solvation can thus be separated. Analysis of the thermodynamic data revealed that the preference for glycine at the C' position of a helix is predominantly a conformational effect.

PubMed: 16446709
DOI: 10.1038/nchembio766

実験手法

X-RAY DIFFRACTION (1.8 Å)