2kx4

Solution structure of Bacteriophage Lambda gpFII

spinqualitylabelsall models 2kx4, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kx4 is a 1 chain structure with sequence from Bacteriophage lambda. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: FII (Bacteriophage lambda) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FII_LAMBD] Plays a role in virion assembly by joining the head and the tail at the last step of morphogenesis. Six FII proteins bind the DNA-filled capsid after W binding, in turn binding the pre-assembled tail by interacting with U protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Evolutionary relationships may exist among very diverse groups of proteins even though they perform different functions and display little sequence similarity. The tailed bacteriophages present a uniquely amenable system for identifying such groups because of their huge diversity yet conserved genome structures. In this work, we used structural, functional, and genomic context comparisons to conclude that the head-tail connector protein and tail tube protein of bacteriophage lambda diverged from a common ancestral protein. Further comparisons of tertiary and quaternary structures indicate that the baseplate hub and tail terminator proteins of bacteriophage may also be part of this same family. We propose that all of these proteins evolved from a single ancestral tail tube protein fold, and that gene duplication followed by differentiation led to the specialized roles of these proteins seen in bacteriophages today. Although this type of evolutionary mechanism has been proposed for other systems, our work provides an evolutionary mechanism for a group of proteins with different functions that bear no sequence similarity. Our data also indicate that the addition of a structural element at the N terminus of the lambda head-tail connector protein endows it with a distinctive protein interaction capability compared with many of its putative homologues. Phages have adapted the same protein fold to fulfill multiple functions in virion assembly.,Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14384-9. Epub 2010 Jul 26. PMID:20660769 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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