Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/37714
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Title

Structure of the functional domain of ø29 replication organizer: insights into oligomerization and DNA binding

AuthorsAsensio, Juan Luis CSIC ORCID; Albert, Armando CSIC ORCID; Muñoz-Espín, D.; González, Carlos CSIC ; Hermoso, José Miguel; Villar, Laurentino CSIC; Jiménez-Barbero, Jesús CSIC ORCID; Salas, Margarita CSIC ORCID ; Meijer, Wilfried J. J. CSIC ORCID
Issue Date27-May-2005
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationThe Journal of Biological Chemistry 280: 20730-20739 (2005)
AbstractThe Bacillus subtilis phage φ29-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.
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M501687200
URIhttp://hdl.handle.net/10261/37714
DOI10.1074/jbc.M501687200
ISSN0021-9258
Appears in Collections:(IQOG) Artículos
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