PDBsum entry 1pdm

Structural protein

PDB id: 1pdm

Contents

Protein chains

(+ 6 more) 328 a.a.* *

* Residue conservation analysis

* C-alpha coords only

PDB id:

1pdm

Name:

Structural protein

Title:

Fitting of gp8 structure into the cryoem reconstruction of the bacteriophage t4 baseplate

Structure:

Baseplate structural protein gp8. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Synonym: baseplate wedge protein 8

Source:

Enterobacteria phage t4. Organism_taxid: 10665

Authors:

V.A.Kostyuchenko,P.G.Leiman,P.R.Chipman,S.Kanamaru,M.J.Van Raaij, F.Arisaka,V.V.Mesyanzhinov,M.G.Rossmann

Key ref:

V.A.Kostyuchenko et al. (2003). Three-dimensional structure of bacteriophage T4 baseplate. Nat Struct Biol, 10, 688-693. PubMed id: 12923574 DOI: 10.1038/nsb970

Date:

19-May-03 Release date: 09-Sep-03

Protein chains

P19062  (BP08_BPT4) -  Baseplate wedge protein gp8 from Enterobacteria phage T4

Seq: 334 a.a.

Struc: 328 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/nsb970

Nat Struct Biol 10:688-693 (2003)

PubMed id: 12923574

Three-dimensional structure of bacteriophage T4 baseplate.

V.A.Kostyuchenko, P.G.Leiman, P.R.Chipman, S.Kanamaru, M.J.van Raaij, F.Arisaka, V.V.Mesyanzhinov, M.G.Rossmann.

ABSTRACT

The baseplate of bacteriophage T4 is a multiprotein molecular machine that controls host cell recognition, attachment, tail sheath contraction and viral DNA ejection. We report here the three-dimensional structure of the baseplate-tail tube complex determined to a resolution of 12 A by cryoelectron microscopy. The baseplate has a six-fold symmetric, dome-like structure approximately 520 A in diameter and approximately 270 A long, assembled around a central hub. A 940 A-long and 96 A-diameter tail tube, coaxial with the hub, is connected to the top of the baseplate. At the center of the dome is a needle-like structure that was previously identified as a cell puncturing device. We have identified the locations of six proteins with known atomic structures, and established the position and shape of several other baseplate proteins. The baseplate structure suggests a mechanism of baseplate triggering and structural transition during the initial stages of T4 infection.

Selected figure(s)

Figure 2.
Figure 2. Fit of the crystal structures, shown as C traces, into the cryoEM density. (a) The short tail fiber gp12 (magenta) and a part of gp11 (cyan) are viewed as area A in Figure 1. (b) gp9 (green), viewed as area B in Figure 1. An intermediate and two extreme directions of the long tail fiber, as suggested by the orientations of the gp9 trimer, are shown as green, red and blue lines, respectively. The orientation of the tail axis is vertical and is situated behind the display.

Figure 3.
Figure 3. Details of the baseplate structure. Proteins are labeled with their respective gene numbers. (a) The garland of short tail fibers gp12 (magenta) with gp11 structures (cyan C -trace) at the kinks of the gp12 fibers. Black line, six-fold axis of the baseplate. (b) The baseplate 'pins,' composed of gp7 (red), gp8 (dark blue C -trace), gp10 (yellow) and gp11 (cyan C -trace). Shown also is gp9 (green C -trace), the long tail fiber attachment protein, with a green line along its three-fold axis representing the direction of the long tail fibers. (c) Unassigned density around the center of the baseplate representing gp6, gp25 and gp53.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2003, 10, 688-693) copyright 2003.

Figures were selected by an automated process.