1OX3

crystal structure of mini-fibritin

1OX3 の概要

• エントリーDOI: 10.2210/pdb1ox3/pdb
• 分子名称: Fibritin (2 entities in total)
• 機能のキーワード: foldon, capping motif, chaperone
• 由来する生物種: Enterobacteria phage T4; 詳細
• 細胞内の位置: Virion : P10104
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11914.26

構造登録者

Boudko, S.P.,Stetefeld, J. (登録日: 2003-04-01, 公開日: 2004-04-13, 最終更新日: 2023-08-16)

主引用文献

Boudko, S.P.,Strelkov, S.V.,Engel, J.,Stetefeld, J.
Design and Crystal Structure of Bacteriophage T4 Mini-Fibritin NCCF.
J.Mol.Biol., 339:927-935, 2004

PubMed Abstract: Fibritin is a fibrous protein that forms "whiskers" attached to the neck of bacteriophage T4. Whiskers interact with the long tail fibers regulating the assembly and infectivity of the virus. The fibritin trimer includes the N-terminal domain responsible for attachment to the phage particle and for the collar formation, the central domain forming a 500 A long segmented coiled-coil structure, and the C-terminal "foldon" domain. We have designed a "mini" fibritin with most of the coiled-coil domain deleted, and solved its crystal structure. The non-helical N-terminal part represents a new protein fold that tightly interacts with the coiled-coil segment forming a single domain, as revealed by calorimetry. The analysis of the crystal structure and earlier electron microscopy data on the collar-whisker complex suggests the necessity of other proteins to participate in the collar formation. Crystal structure determination of the N-terminal domain of fibritin is the first step towards elucidating the detailed structure and assembly mechanism of the collar-whisker complex.

PubMed: 15165860
DOI: 10.1016/j.jmb.2004.04.001

実験手法

X-RAY DIFFRACTION (2 Å)