1NO4

Crystal Structure of the pre-assembly scaffolding protein gp7 from the double-stranded DNA bacteriophage phi29

1NO4 の概要

• エントリーDOI: 10.2210/pdb1no4/pdb
• 関連するPDBエントリー: 1NOH
• 分子名称: HEAD MORPHOGENESIS PROTEIN (2 entities in total)
• 機能のキーワード: coiled-coil, viral protein
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44661.44

構造登録者

Morais, M.C.,Kanamaru, S.,Badasso, M.O.,Koti, J.S.,Owen, B.A.L.,McMurray, C.T.,Anderson, D.L.,Rossmann, M.G. (登録日: 2003-01-15, 公開日: 2003-07-01, 最終更新日: 2024-02-14)

主引用文献

Morais, M.C.,Kanamaru, S.,Badasso, M.O.,Koti, J.S.,Owen, B.A.L.,McMurray, C.T.,Anderson, D.L.,Rossmann, M.G.
Bacteriophage f29 scaffolding protein gp7 before and after prohead assembly
Nat.Struct.Biol., 10:572-576, 2003

PubMed Abstract: Three-dimensional structures of the double-stranded DNA bacteriophage phi29 scaffolding protein (gp7) before and after prohead assembly have been determined at resolutions of 2.2 and 2.8 A, respectively. Both structures are dimers that resemble arrows, with a four-helix bundle composing the arrowhead and a coiled coil forming the tail. The structural resemblance of gp7 to the yeast transcription factor GCN4 suggests a DNA-binding function that was confirmed by native gel electrophoresis. DNA binding to gp7 may have a role in mediating the structural transition from prohead to mature virus and scaffold release. A cryo-EM analysis indicates that gp7 is arranged inside the capsid as a series of concentric shells. The position of the higher density features in these shells correlates with the positions of hexamers in the equatorial region of the capsid, suggesting that gp7 may regulate formation of the prolate head through interactions with these hexamers.

PubMed: 12778115
DOI: 10.1038/nsb939

実験手法

X-RAY DIFFRACTION (2.2 Å)