2bnk

The structure of phage phi29 replication organizer protein p16.7

spinqualitylabelsall models 2bnk, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bnk is a 2 chain structure with sequence from Bacillus virus phi29. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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:11741949) (PubMed:11169113). 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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