2WW6

foldon containing D-amino acids in turn positions

2WW6 の概要

• エントリーDOI: 10.2210/pdb2ww6/pdb
• 関連するPDBエントリー: 2WW7
• 分子名称: FIBRITIN, TETRAETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: d-amino acids, chaperone, viral protein
• 由来する生物種: ENTEROBACTERIA PHAGE T4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 9585.94

構造登録者

Eckhardt, B.,Grosse, W.,Essen, L.-O.,Geyer, A. (登録日: 2009-10-22, 公開日: 2010-09-29, 最終更新日: 2024-11-06)

主引用文献

Eckhardt, B.,Grosse, W.,Essen, L.,Geyer, A.
Structural Characterization of a Beta-Turn Mimic within a Protein-Protein Interface.
Proc.Natl.Acad.Sci.USA, 107:18336-, 2010

PubMed Abstract: β-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic β-turn mimics as parts of surface-exposed loops. A β-turn mimic, Hot═Tap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot═Tap dipeptide proved its strong β-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot═Tap hybrid reveal at atomic resolution how Hot═Tap replaces a βI'-turn by a βII'-type structure. Furthermore, Hot═Tap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, β-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins.

PubMed: 20937907
DOI: 10.1073/PNAS.1004187107

実験手法

X-RAY DIFFRACTION (0.98 Å)