Structural highlights
Function
[FII_LAMBD] Plays a role in virion assembly by joining the head and the tail at the last step of morphogenesis. Six FII proteins bind the DNA-filled capsid after W binding, in turn binding the pre-assembled tail by interacting with U protein.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The bacteriophage lambda FII protein (gpFII) is a 117 residue structural protein found in the phage particle that is required for the joining of phage heads and tails at the last step of morphogenesis. We have performed biophysical experiments to show that gpFII is stable, monomeric, and reversibly folded. We have also determined the atomic resolution structure of gpFII using NMR spectroscopy. gpFII is shown to possess a novel fold consisting of seven beta-strands and a short alpha-helix. It also displays two large unstructured regions at the N terminus (residues 1-24) and in a large loop near the middle of the protein (residues 46-62). We speculate that these unstructured regions become structured when gpFII assembles into the phage particle, and that these conformational changes play an important role in regulating the assembly pathway. Alignment of the gpFII sequence with those of homologues from other lambdoid phages has allowed us to putatively identify distinct surfaces on the gpFII structure that mediate binding to the phage head and tail.
The solution structure of the bacteriophage lambda head-tail joining protein, gpFII.,Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR J Mol Biol. 2002 May 17;318(5):1395-404. PMID:12083526[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boklage CE, Wong EC, Bode VC. Functional abnormality of lambda phage particles from complemented FII-mutant lysates. Virology. 1974 Sep;61(1):22-8. PMID:4413519
- ↑ Casjens S. Bacteriophage lambda FII gene protein: role in head assembly. J Mol Biol. 1974 Nov 25;90(1):1-20. PMID:4616093
- ↑ Casjens S, Horn T, Kaiser AD. Head assembly steps controlled by genes F and W in bacteriophage lambda. J Mol Biol. 1972 Mar 14;64(3):551-63. PMID:5022189
- ↑ Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR. The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. J Mol Biol. 2002 May 17;318(5):1395-404. PMID:12083526
