1no4
From Proteopedia
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Crystal Structure of the pre-assembly scaffolding protein gp7 from the double-stranded DNA bacteriophage phi29
Overview
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.
About this Structure
1NO4 is a Single protein structure of sequence from Vibrio phage f237. Full crystallographic information is available from OCA.
Reference
Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly., Morais MC, Kanamaru S, Badasso MO, Koti JS, Owen BA, McMurray CT, Anderson DL, Rossmann MG, Nat Struct Biol. 2003 Jul;10(7):572-6. PMID:12778115
Page seeded by OCA on Tue Nov 20 22:25:15 2007
