1g3p
From Proteopedia
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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 mu with as ligand. 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
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