PDBsum entry 1s2e

Viral protein

PDB id: 1s2e

Contents

Protein chains

288 a.a. *

Ligands

EPE ×2

Waters ×292

* Residue conservation analysis

PDB id:

1s2e

Name:

Viral protein

Title:

Bacteriophage t4 gene product 9 (gp9), the trigger of tail contraction and the long tail fibers connector, alternative fit of the first 19 residues

Structure:

Baseplate structural protein gp9. Chain: a, b. Synonym: baseplate wedge protein 9. Engineered: yes

Source:

Enterobacteria phage t4. Organism_taxid: 10665. Gene: 9. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.30Å R-factor: 0.239 R-free: 0.277

Authors:

V.A.Kostyuchenko,G.A.Navruzbekov,L.P.Kurochkina,S.V.Strelkov, V.V.Mesyanzhinov,M.G.Rossmann

Key ref:

V.A.Kostyuchenko et al. (1999). The structure of bacteriophage T4 gene product 9: the trigger for tail contraction. Structure, 7, 1213-1222. PubMed id: 10545330 DOI: 10.1016/S0969-2126(00)80055-6

Date:

08-Jan-04 Release date: 13-Jan-04

Protein chains

P10927  (BP09_BPT4) -  Baseplate protein gp9 from Enterobacteria phage T4

Seq: 288 a.a.

Struc: 288 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/S0969-2126(00)80055-6

Structure 7:1213-1222 (1999)

PubMed id: 10545330

The structure of bacteriophage T4 gene product 9: the trigger for tail contraction.

V.A.Kostyuchenko, G.A.Navruzbekov, L.P.Kurochkina, S.V.Strelkov, V.V.Mesyanzhinov, M.G.Rossmann.

ABSTRACT

BACKGROUND: The T4 bacteriophage consists of a head, filled with double-stranded DNA, and a complex contractile tail required for the ejection of the viral genome into the Escherichia coli host. The tail has a baseplate to whïch are attached six long and six short tail fibers. These fibers are the sensing devices for recognizing the host. When activated by attachment to cell receptors, the fibers cause a conformational transition in the baseplate and subsequently in the tail sheath, which initiates DNA ejection. The baseplate is a multisubunit complex of proteins encoded by 15 genes. Gene product 9 (gp9) is the protein that connects the long tail fibers to the baseplate and triggers the tail contraction after virus attachment to a host cell. RESULTS: The crystal structure of recombinant gp9, determined to 2.3 A resolution, shows that the protein of 288 amino acid residues assembles as a homotrimer. The monomer consists of three domains: the N-terminal domain generates a triple coiled coil; the middle domain is a mixed, seven-stranded beta sandwich with a topology not previously observed; and the C-terminal domain is an eight-stranded, antiparallel beta sandwich having some resemblance to 'jelly-roll' viral capsid protein structures. CONCLUSIONS: The biologically active form of gp9 is a trimer. The protein contains flexible interdomain hinges, which are presumably required to facilitate signal transmission between the long tail fibers and the baseplate. Structural and genetic analyses show that the C-terminal domain is bound to the baseplate, and the N-terminal coiled-coil domain is associated with the long tail fibers.

Selected figure(s)

Figure 4.
Figure 4. Topology diagrams for (a) the middle domain and (b) the C-terminal domain. (c) Topology of a jelly-roll fold, as occurs in many viral capsid proteins. (d) The b-annulus connecting the middle and C-terminal domains. The amino acids and hydrogen bonding between subunits A, B and C are shown.

The above figure is reprinted by permission from Cell Press: Structure (1999, 7, 1213-1222) copyright 1999.

Figure was selected by an automated process.