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TitleEvolution of bacteriophage tails: Structure of T4 gene product 10.
Journal, issue, pagesJ Mol Biol, Vol. 358, Issue 3, Page 912-921, Year 2006
Publish dateMay 5, 2006
AuthorsPetr G Leiman / Mikhail M Shneider / Vadim V Mesyanzhinov / Michael G Rossmann /
PubMed AbstractThe success of tailed bacteriophages to infect cells far exceeds that of most other viruses on account of their specialized tail and associated baseplate structures. The baseplate protein gene ...The success of tailed bacteriophages to infect cells far exceeds that of most other viruses on account of their specialized tail and associated baseplate structures. The baseplate protein gene product (gp) 10 of bacteriophage T4, whose structure was determined to 1.2 A resolution, was fitted into the cryo-electron microscopy structures of the pre and post-infection conformations of the virus. gp10 functions as a molecular lever that rotates and extends the hinged short tail fibers to facilitate cell attachment. The central folding motif of the gp10 trimer is similar to that of the baseplate protein gp11 and to the receptor-binding domain of the short tail fiber, gp12. The three proteins comprise the periphery of the baseplate and interact with each other. The structural and functional similarities of gp10, gp11, and gp12 and their sequential order in the T4 genome suggest that they evolved separately, subsequent to gene triplication from a common ancestor. Such events are usual in the evolution of complex organelles from a common primordial molecule.
External linksJ Mol Biol / PubMed:16554069
MethodsX-ray diffraction / EM (single particle)
Resolution1.2 - 17 Å
Structure data

PDB-2fkk:
Crystal structure of the C-terminal domain of the bacteriophage T4 gene product 10
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-2fl8:
Fitting of the gp10 trimer structure into the cryoEM map of the bacteriophage T4 baseplate in the hexagonal conformation.
Method: ELECTRON MICROSCOPY / Resolution: 12 Å

PDB-2fl9:
Evolution of bacteriophage tails: Structure of T4 gene product 10
Method: ELECTRON MICROSCOPY / Resolution: 17 Å

Chemicals

ChemComp-BR:
BROMIDE ION

ChemComp-PO3:
PHOSPHITE ION

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t4 (virus)
KeywordsVIRAL PROTEIN / Bacteriophage T4; Baseplate; Tail; Evolution; gp10; Structural comparisons / VIRUS/VIRAL PROTEIN / VIRUS-VIRAL PROTEIN COMPLEX

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