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Structure of the bacterial replication origin-associated protein Cnu
Structural highlights
FunctionCNU_ECOLI The complex formed with H-NS binds to the specific 26-bp cnb site in the origin of replication oriC. Can complement, at least partially, the absence of the Hha protein in hha mutants.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCnu is a nucleoid protein that has a high degree of sequence homology with Hha/YmoA family proteins, which bind to chromatin and regulate the expression of Escherichia coli virulence genes in response to changes in temperature or ionic strength. Here, we determined its solution structure and dynamic properties and mapped H-NS binding sites. Cnu consists of three alpha helices that are comparable with those of Hha, but it has significant flexibility in the C-terminal region and lacks a short alpha helix present in Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the ends of the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structural platform for H-NS binding. Our results may provide structural and dynamic bases for the similarity and dissimilarity between Cnu and Hha functions. Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha.,Bae SH, Liu D, Lim HM, Lee Y, Choi BS Biochemistry. 2008 Feb 19;47(7):1993-2001. Epub 2008 Jan 12. PMID:18189420[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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