5MNT

Bacteriophage Qbeta maturation protein

5MNT の概要

• エントリーDOI: 10.2210/pdb5mnt/pdb
• 分子名称: A2 maturation protein (1 entity in total)
• 機能のキーワード: virus attachment, minor capsid protein, rna binding protein
• 由来する生物種: Enterobacteria phage Qbeta
• 細胞内の位置: Virion : Q8LTE2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 194504.05

構造登録者

Rumnieks, J.,Tars, K. (登録日: 2016-12-13, 公開日: 2017-01-11, 最終更新日: 2024-05-08)

主引用文献

Rumnieks, J.,Tars, K.
Crystal Structure of the Maturation Protein from Bacteriophage Q beta.
J. Mol. Biol., 429:688-696, 2017

PubMed Abstract: Virions of the single-stranded RNA bacteriophages contain a single copy of the maturation protein, which is bound to the phage genome and is required for the infectivity of the particles. The maturation protein mediates the adsorption of the virion to bacterial pili and the subsequent release and penetration of the genome into the host cell. Here, we report a crystal structure of the maturation protein from bacteriophage Qβ. The protein has a bent, highly asymmetric shape and spans 110Å in length. Apart from small local substructures, the overall fold of the maturation protein does not resemble that of other known proteins. The protein is organized in two distinct regions, an α-helical part with a four-helix core, and a β stranded part that contains a seven-stranded sheet in the central part and a five-stranded sheet at the tip of the protein. The Qβ maturation protein has two distinct, positively charged areas at opposite sides of the α-helical part, which are involved in genomic RNA binding. The maturation protein binds to each of the surrounding coat protein dimers in the capsid differently, and the interaction is considerably weaker compared to coat protein interdimer contacts. The coat protein- or RNA-binding residues are not preserved among different ssRNA phage maturation proteins; instead, the distal end of the α-helical part is the most evolutionarily conserved, suggesting the importance of this region for maintaining the functionality of the protein.

PubMed: 28111107
DOI: 10.1016/j.jmb.2017.01.012

実験手法

X-RAY DIFFRACTION (3.32 Å)