PDBsum entry 2fl8

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Virus/viral protein PDB id
Protein chains
(+ 12 more) 344 a.a.* *
* Residue conservation analysis
* C-alpha coords only
PDB id:
Name: Virus/viral protein
Title: Fitting of the gp10 trimer structure into the cryoem map of bacteriophage t4 baseplate in the hexagonal conformation.
Structure: Baseplate structural protein gp10. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r synonym: baseplate wedge protein 10. Engineered: yes. Mutation: yes
Source: Enterobacteria phage t4. Organism_taxid: 10665. Strain: d. Gene: 10. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: 80mer (from PQS)
Authors: P.G.Leiman,M.M.Shneider,V.V.Mesyanzhinov,M.G.Rossmann
Key ref:
P.G.Leiman et al. (2006). Evolution of bacteriophage tails: Structure of T4 gene product 10. J Mol Biol, 358, 912-921. PubMed id: 16554069 DOI: 10.1016/j.jmb.2006.02.058
05-Jan-06     Release date:   04-Apr-06    

Protein chains
Pfam   ArchSchema ?
P10928  (VG10_BPT4) -  Base plate structural protein gp10
602 a.a.
344 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     virion   1 term 
  Biological process     viral infectious cycle   1 term 


    Key reference    
DOI no: 10.1016/j.jmb.2006.02.058 J Mol Biol 358:912-921 (2006)
PubMed id: 16554069  
Evolution of bacteriophage tails: Structure of T4 gene product 10.
P.G.Leiman, M.M.Shneider, V.V.Mesyanzhinov, M.G.Rossmann.
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.
  Selected figure(s)  
Figure 5.
Figure 5. Stereo diagrams showing the fit of the gp10_397C crystal structure (labeled as 10C) and the gp10 N-terminal domain model (labeled as 10N) into the cryoEM density of the baseplate. The gp10 N-terminal domain model was based on its homology with the N-terminal and middle domains of gp9. (a) A 45° tilted view of the hexagonal conformation of the baseplate. (b) A 45°tilted view of the star-shaped conformation. The black line indicates the 6-fold axis of the baseplate. Only two asymmetric units of the baseplate are shown for clarity. The proteins are labeled with their corresponding gene numbers. The cryoEM densities corresponding to gp8, gp9, and gp11 have been interpreted in terms of their known atomic structures, which are shown as C^a traces and are colored green (gp9), light blue (gp8), dark blue (gp10_397C), purple (gp10 N-terminal domain), cyan (gp11), and magenta (gp12 C-terminal domain). The cryoEM densities corresponding to gp7, gp10, and gp12 are colored red, yellow, and gray, respectively. The termini of gp12 are indicated as 12N and 12C. The three domains of gp7 are labeled with letters A, B, and C.
Figure 6.
Figure 6. Molecular surfaces of gp9, gp10, and gp12 showing the interactions between the proteins with known atomic structures in the two conformations of the baseplate. The dotted line indicates the 2-fold axis by which gp10 has been rotated away from gp12 (top) or gp9 (bottom) in order to open up the interacting surfaces. The interacting residues are labeled and highlighted with colors based on their biochemical properties: hydrophobic, yellow; polar, cyan; negatively charged, red; positively charged, blue. (a) Interactions between gp10 and gp12 in the hexagonal baseplate. (b) Interactions between gp9 and gp10 in the star-shaped baseplate.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 358, 912-921) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20593364 M.L.Yap, K.Mio, S.Ali, A.Minton, S.Kanamaru, and F.Arisaka (2010).
Sequential assembly of the wedge of the baseplate of phage T4 in the presence and absence of gp11 as monitored by analytical ultracentrifugation.
  Macromol Biosci, 10, 808-813.  
  21129200 P.G.Leiman, F.Arisaka, M.J.van Raaij, V.A.Kostyuchenko, A.A.Aksyuk, S.Kanamaru, and M.G.Rossmann (2010).
Morphogenesis of the T4 tail and tail fibers.
  Virol J, 7, 355.  
21041684 S.G.Bartual, J.M.Otero, C.Garcia-Doval, A.L.Llamas-Saiz, R.Kahn, G.C.Fox, and M.J.van Raaij (2010).
Structure of the bacteriophage T4 long tail fiber receptor-binding tip.
  Proc Natl Acad Sci U S A, 107, 20287-20292.
PDB code: 2xgf
17395453 J.E.Johnson, and W.Chiu (2007).
DNA packaging and delivery machines in tailed bacteriophages.
  Curr Opin Struct Biol, 17, 237-243.  
17164521 M.G.Rossmann, F.Arisaka, A.J.Battisti, V.D.Bowman, P.R.Chipman, A.Fokine, S.Hafenstein, S.Kanamaru, V.A.Kostyuchenko, V.V.Mesyanzhinov, M.M.Shneider, M.C.Morais, P.G.Leiman, L.M.Palermo, C.R.Parrish, and C.Xiao (2007).
From structure of the complex to understanding of the biology.
  Acta Crystallogr D Biol Crystallogr, 63, 9.  
17660435 T.T.Pham, D.Jacobs-Sera, M.L.Pedulla, R.W.Hendrix, and G.F.Hatfull (2007).
Comparative genomic analysis of mycobacteriophage Tweety: evolutionary insights and construction of compatible site-specific integration vectors for mycobacteria.
  Microbiology, 153, 2711-2723.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.