3H2T: Crystal structure of gene product 6, baseplate protein of bacteriophage T4

Citation:
Abstract
The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring.
PDB ID: 3H2TDownload
MMDB ID: 72812
PDB Deposition Date: 2009/4/14
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 3.2  Å
Source Organism:
Similar Structures:
Biological Unit for 3H2T: dimeric; determined by author and by software (PISA)
Molecular Components in 3H2T
Label Count Molecule
Proteins (2 molecules)
2
Baseplate Structural Protein GP6(Gene symbol: 6)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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