2l04

The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube ProteinThe Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein

Structural highlights 2l04 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: V (Bacteriophage lambda) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VMTV_LAMBD] Protein forming the phage's tail tube, which is composed of about 32 hexameric disks. There are 135-212 copies of gene V protein per mature phage. Probably undergoes structural rearrangements leading to injection of the phage DNA into the host (By similarity). 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 Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpV(C)), the tail tube protein of phage lambda. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpV(C) and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpV(C) by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpV(C) structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpV(C) that may be important in mediating the function of this domain. The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage lambda Tail Tube Protein.,Pell LG, Gasmi-Seabrook GM, Morais M, Neudecker P, Kanelis V, Bona D, Donaldson LW, Edwards AM, Howell PL, Davidson AR, Maxwell KL J Mol Biol. 2010 Sep 6. PMID:20826161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2l04, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image