This entry corresponds to the N-terminal oligomerisation domain of H-NS histone-like proteins. Paper describing PDB structure 1lr1. [1]. 12460581. H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein. Esposito D, Petrovic A, Harris R, Ono S, Eccleston JF, Mbabaali A, Haq I, Higgins CF, Hinton JC, Driscoll PC, Ladbury JE;. J Mol Biol. 2002;324:841-850. Paper describing PDB structure 1ni8. [2]. 12592399. The H-NS dimerization domain defines a new fold contributing to DNA recognition. Bloch V, Yang Y, Margeat E, Chavanieu A, Auge MT, Robert B, Arold S, Rimsky S, Kochoyan M;. Nat Struct Biol. 2003;10:212-218. Paper describing PDB structure 1ov9. [3]. 14607110. Crystal structure of the N-terminal dimerisation domain of VicH, the H-NS-like protein of Vibrio cholerae. Cerdan R, Bloch V, Yang Y, Bertin P, Dumas C, Rimsky S, Kochoyan M, Arold ST;. J Mol Biol. 2003;334:179-185. Paper describing PDB structure 2mw2. [4]. 26085102. A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing. Cordeiro TN, Garcia J, Bernado P, Millet O, Pons M;. J Biol Chem. 2015;290:21200-21212. Paper describing PDB structure 3nr7. [5]. 20798056. H-NS forms a superhelical protein scaffold for DNA condensation. Arold ST, Leonard PG, Parkinson GN, Ladbury JE;. Proc Natl Acad Sci U S A. 2010;107:15728-15732. (from Pfam)
- Date:
- 2024-10-16