2JTM
Solution structure of Sso6901 from Sulfolobus solfataricus P2
Summary for 2JTM
| Entry DOI | 10.2210/pdb2jtm/pdb |
| NMR Information | BMRB: 15415 |
| Descriptor | Putative uncharacterized protein (1 entity in total) |
| Functional Keywords | sh3-like, dna binding protein |
| Biological source | Sulfolobus solfataricus |
| Total number of polymer chains | 1 |
| Total formula weight | 6677.91 |
| Authors | |
| Primary citation | Guo, L.,Feng, Y.,Zhang, Z.,Yao, H.,Luo, Y.,Wang, J.,Huang, L. Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea Nucleic Acids Res., 36:1129-1137, 2008 Cited by PubMed Abstract: Archaea contain a variety of chromatin proteins consistent with the evolution of different genome packaging mechanisms. Among the two main kingdoms in the Archaea, Euryarchaeota synthesize histone homologs, whereas Crenarchaeota have not been shown to possess a chromatin protein conserved at the kingdom level. We report the identification of Cren7, a novel family of chromatin proteins highly conserved in the Crenarchaeota. A small, basic, methylated and abundant protein, Cren7 displays a higher affinity for double-stranded DNA than for single-stranded DNA, constrains negative DNA supercoils and is associated with genomic DNA in vivo. The solution structure and DNA-binding surface of Cren7 from the hyperthermophilic crenarchaeon Sulfolobus solfataricus were determined by NMR. The protein adopts an SH3-like fold. It interacts with duplex DNA through a beta-sheet and a long flexible loop, presumably resulting in DNA distortions through intercalation of conserved hydrophobic residues into the DNA structure. These data suggest that the crenarchaeal kingdom in the Archaea shares a common strategy in chromatin organization. PubMed: 18096617DOI: 10.1093/nar/gkm1128 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
