| Structural highlights
Function
GP167_BPPH2 Binds to the long stretches of ssDNA of the viral DNA replication intermediates created during the protein-primed mechanism of replication of the viral genome and attaches the viral DNA to the membrane of the infected cells (PubMed:11169113, PubMed:11741949). Required for the redistribution of replicating viral DNA from the initial replication site to membrane-associated sites surrounding the nucleoid (PubMed:10921898). Required for the second pull step of DNA ejection (PubMed:17526715).[1] [2] [3] [4]
Publication Abstract from PubMed
The Bacillus subtilis phage phi29-encoded membrane protein p16.7 is one of the few proteins involved in prokaryotic membrane-associated DNA replication that has been characterized at a functional and biochemical level. In this work we have determined both the solution and crystal structures of its dimeric functional domain, p16.7C. Although the secondary structure of p16.7C is remarkably similar to that of the DNA binding homeodomain, present in proteins belonging to a large family of eukaryotic transcription factors, the tertiary structures of p16.7C and homeodomains are fundamentally different. In fact, p16.7C defines a novel dimeric six-helical fold. We also show that p16.7C can form multimers in solution and that this feature is a key factor for efficient DNA binding. Moreover, a combination of NMR and x-ray approaches, combined with functional analyses of mutants, revealed that multimerization of p16.7C dimers is mediated by a large protein surface that is characterized by a striking self-complementarity. Finally, the structural analyses of the p16.7C dimer and oligomers provide important clues about how protein multimerization and DNA binding are coupled.
Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding.,Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:15772069[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meijer WJ, Lewis PJ, Errington J, Salas M. Dynamic relocalization of phage phi 29 DNA during replication and the role of the viral protein p16.7. EMBO J. 2000 Aug 1;19(15):4182-90. PMID:10921898 doi:10.1093/emboj/19.15.4182
- ↑ Meijer WJ, Serna-Rico A, Salas M. Characterization of the bacteriophage phi29-encoded protein p16.7: a membrane protein involved in phage DNA replication. Mol Microbiol. 2001 Feb;39(3):731-46. PMID:11169113 doi:10.1046/j.1365-2958.2001.02260.x
- ↑ Serna-Rico A, Salas M, Meijer WJ. The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA replication, is a membrane-localized single-stranded DNA-binding protein. J Biol Chem. 2002 Feb 22;277(8):6733-42. PMID:11741949 doi:10.1074/jbc.M109312200
- ↑ Alcorlo M, González-Huici V, Hermoso JM, Meijer WJ, Salas M. The phage phi29 membrane protein p16.7, involved in DNA replication, is required for efficient ejection of the viral genome. J Bacteriol. 2007 Aug;189(15):5542-9. PMID:17526715 doi:10.1128/JB.00402-07
- ↑ Asensio JL, Albert A, Munoz-Espin D, Gonzalez C, Hermoso J, Villar L, Jimenez-Barbero J, Salas M, Meijer WJ. Structure of the functional domain of phi29 replication organizer: insights into oligomerization and dna binding. J Biol Chem. 2005 May 27;280(21):20730-9. Epub 2005 Mar 16. PMID:15772069 doi:M501687200
|
