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1g3p
From Proteopedia
CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P
Overview
The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.
About this Structure
1G3P is a Single protein structure of sequence from Enterobacteria phage m13. Full crystallographic information is available from OCA.
Reference
The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p., Lubkowski J, Hennecke F, Pluckthun A, Wlodawer A, Nat Struct Biol. 1998 Feb;5(2):140-7. PMID:9461080 Page seeded by OCA on Fri May 2 17:05:57 2008
