9e7m

Structural highlights

Function

TMP_LAMBD Serves as a ruler that controls the length of tail by stopping the tail tube polymerization and is probably released from the tail shaft during infection to facilitate DNA translocation into the host cell (PubMed:2150582). Assembles into a multimeric linear form possibly stabilized by the covering tail assembly proteins G and GT (PubMed:23911548). Its C-terminus fixes the tail tip complex (J, I, L, K), thereby forming the tail assembly initiator complex (PubMed:23911548). Tail tube proteins polymerize around tape measure protein, displacing the tail assembly protein G and GT (PubMed:23911548). When the tail reaches the length specified by the tape measure protein, it stops and becomes capped by the tail terminator protein (Probable). Upon tail assembly, tape measure protein is cleaved into a form called H*, that plays a role later during virion entry in a new cell (Probable). Once assembled, the virion is released and can infect new cells by binding to the entry receptor LambB (Probable). After opening of a pore on the external membrane, the entry protein H* protein is probably released in the periplasmic space for successful DNA injection (PubMed:23911548).[HAMAP-Rule:MF_04138]^{[1] [2] [3] [4] [5] [6] [7]}

References

1. ↑ Katsura I. Mechanism of length determination in bacteriophage lambda tails. Adv Biophys. 1990;26:1-18. doi: 10.1016/0065-227x(90)90004-d. PMID:2150582 doi:http://dx.doi.org/10.1016/0065-227x(90)90004-d
2. ↑ Xu J, Hendrix RW, Duda RL. Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length. J Mol Biol. 2014 Mar 6;426(5):1004-18. doi: 10.1016/j.jmb.2013.06.040. Epub 2013 , Jul 30. PMID:23911548 doi:http://dx.doi.org/10.1016/j.jmb.2013.06.040
3. ↑ Xu J, Hendrix RW, Duda RL. Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length. J Mol Biol. 2014 Mar 6;426(5):1004-18. doi: 10.1016/j.jmb.2013.06.040. Epub 2013 , Jul 30. PMID:23911548 doi:http://dx.doi.org/10.1016/j.jmb.2013.06.040
4. ↑ Scandella D, Arber W. Phage lambda DNA injection into Escherichia coli pel mutations in phage genes V or H. Virology. 1976 Jan;69(1):206-15. PMID:1108413 doi:10.1016/0042-6822(76)90207-5
5. ↑ Xu J, Hendrix RW, Duda RL. Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length. J Mol Biol. 2014 Mar 6;426(5):1004-18. doi: 10.1016/j.jmb.2013.06.040. Epub 2013 , Jul 30. PMID:23911548 doi:http://dx.doi.org/10.1016/j.jmb.2013.06.040
6. ↑ Tsui LC, Hendrix RW. Proteolytic processing of phage lambda tail protein gpH: timing of the cleavage. Virology. 1983 Mar;125(2):257-64. PMID:6220513 doi:10.1016/0042-6822(83)90199-x
7. ↑ Roessner CA, Ihler GM. Proteinase sensitivity of bacteriophage lambda tail proteins gpJ and pH in complexes with the lambda receptor. J Bacteriol. 1984 Jan;157(1):165-70. PMID:6228546 doi:10.1128/jb.157.1.165-170.1984