2BNK
The structure of phage phi29 replication organizer protein p16.7
Summary for 2BNK
Entry DOI | 10.2210/pdb2bnk/pdb |
Descriptor | EARLY PROTEIN GP16.7 (2 entities in total) |
Functional Keywords | dna-binding protein, dna binding protein |
Biological source | BACILLUS PHAGE PHI29 |
Total number of polymer chains | 2 |
Total formula weight | 15875.94 |
Authors | Albert, A.,Asensio, J.L.,Munoz-Espin, D.,Gonzalez, C.,Hermoso, J.A.,Villar, L.,Jimenez-Barbero, J.,Salas, M.,Meijer, W.J.J. (deposition date: 2005-03-28, release date: 2005-04-05, Last modification date: 2024-05-08) |
Primary citation | Asensio, J.L.,Albert, A.,Munoz-Espin, D.,Gonzalez, C.,Hermoso, J.A.,Villar, L.,Jimenez-Barbero, J.,Salas, M.,Meijer, W.J.J. Structure of the Functional Domain of {Varphi}29 Replication Organizer: Insights Into Oligomerization and DNA Binding. J.Biol.Chem., 280:20730-, 2005 Cited by PubMed Abstract: 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. PubMed: 15772069DOI: 10.1074/JBC.M501687200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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