1NO4

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

Summary for 1NO4

• Entry DOI: 10.2210/pdb1no4/pdb
• Related: 1NOH
• Descriptor: HEAD MORPHOGENESIS PROTEIN (2 entities in total)
• Functional Keywords: coiled-coil, viral protein
• Biological source: Bacillus phage phi29
• Total number of polymer chains: 4
• Total formula weight: 44661.44

Authors

Morais, M.C.,Kanamaru, S.,Badasso, M.O.,Koti, J.S.,Owen, B.A.L.,McMurray, C.T.,Anderson, D.L.,Rossmann, M.G. (deposition date: 2003-01-15, release date: 2003-07-01, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)