2JQT
Structure of the bacterial replication origin-associated protein Cnu
Summary for 2JQT
| Entry DOI | 10.2210/pdb2jqt/pdb |
| Related | 1jw2 |
| Descriptor | H-NS/stpA-binding protein 2 (1 entity in total) |
| Functional Keywords | cnu, ydgt, replication origin associated, oric, h-ns, protein binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 8428.57 |
| Authors | Bae, S.H.,Liu, D.,Lim, H.M.,Lee, Y.,Choi, B.S. (deposition date: 2007-06-07, release date: 2008-04-22, Last modification date: 2023-12-20) |
| Primary citation | Bae, S.H.,Liu, D.,Lim, H.M.,Lee, Y.,Choi, B.S. Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha. Biochemistry, 47:1993-2001, 2008 Cited by PubMed 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. PubMed: 18189420DOI: 10.1021/bi701914t PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
