3GQA

Crystal Structure of the Bacteriophage phi29 gene product 12 N-terminal fragment in complex with cobalt ions

3GQA の概要

• エントリーDOI: 10.2210/pdb3gqa/pdb
• 関連するPDBエントリー: 3GQ7 3GQ8 3GQ9 3GQH 3GQK 3GQN
• 分子名称: Preneck appendage protein, COBALT (II) ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: beta helix, viral protein
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64623.75

構造登録者

Xiang, Y.,Rossmann, M.G. (登録日: 2009-03-24, 公開日: 2009-05-26, 最終更新日: 2023-09-06)

主引用文献

Xiang, Y.,Leiman, P.G.,Li, L.,Grimes, S.,Anderson, D.L.,Rossmann, M.G.
Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.
Mol.Cell, 34:375-386, 2009

PubMed Abstract: The tailed bacteriophage phi29 has 12 "appendages" (gene product 12, gp12) attached to its neck region that participate in host cell recognition and entry. In the cell, monomeric gp12 undergoes proteolytic processing that releases the C-terminal domain during assembly into trimers. We report here crystal structures of the protein before and after catalytic processing and show that the C-terminal domain of gp12 is an "autochaperone" that aids trimerization. We also show that autocleavage of the C-terminal domain is a posttrimerization event that is followed by a unique ATP-dependent release. The posttranslationally modified N-terminal part has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids, and bind irreversibly to the host, respectively. Structural and sequence comparisons suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins might have a similar maturation mechanism as is performed by phi29 gp12 for Bacillus subtilis.

PubMed: 19450535
DOI: 10.1016/j.molcel.2009.04.009

実験手法

X-RAY DIFFRACTION (2.1 Å)