2JQT: Structure of the bacterial replication origin-associated protein Cnu

Citation:
Abstract
Cnu 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.
PDB ID: 2JQTDownload
MMDB ID: 63882
PDB Deposition Date: 2007/6/7
Updated in MMDB: 2009/07
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2JQT
Label Count Molecule
Protein (1 molecule)
1
H-ns/stpa-binding Protein 2(Gene symbol: cnu)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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