2L04

The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein

2L04 の概要

• エントリーDOI: 10.2210/pdb2l04/pdb
• NMR情報: BMRB: 17028
• 分子名称: Major tail protein V (1 entity in total)
• 機能のキーワード: bacteriophage lambda, phage tail, gpv, ig-like domain, viral protein
• 由来する生物種: Enterobacteria phage lambda (Bacteriophage lambda)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8882.02

構造登録者

Pell, L.G.,Gasmi-Seabrook, G.M.C.,Donaldson, L.W.,Howell, P.,Davidson, A.R.,Maxwell, K.L. (登録日: 2010-06-30, 公開日: 2010-09-22, 最終更新日: 2024-05-01)

主引用文献

Pell, L.G.,Gasmi-Seabrook, G.M.,Morais, M.,Neudecker, P.,Kanelis, V.,Bona, D.,Donaldson, L.W.,Edwards, A.M.,Howell, P.L.,Davidson, A.R.,Maxwell, K.L.
The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage l Tail Tube Protein.
J.Mol.Biol., 403:468-479, 2010

PubMed Abstract: Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpV(C)), the tail tube protein of phage λ. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpV(C) and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpV(C) by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpV(C) structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpV(C) that may be important in mediating the function of this domain.

PubMed: 20826161
DOI: 10.1016/j.jmb.2010.08.044

実験手法

SOLUTION NMR