1SSO
SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS SOLFATARICUS
Summary for 1SSO
| Entry DOI | 10.2210/pdb1sso/pdb |
| NMR Information | BMRB: 5909,5910 |
| Descriptor | SSO7D (1 entity in total) |
| Functional Keywords | dna-binding protein, dna binding protein |
| Biological source | Sulfolobus solfataricus |
| Total number of polymer chains | 1 |
| Total formula weight | 7034.22 |
| Authors | Baumann, H.,Knapp, S.,Lundback, T.,Ladenstein, R.,Hard, T. (deposition date: 1995-03-31, release date: 1995-05-08, Last modification date: 2024-05-22) |
| Primary citation | Baumann, H.,Knapp, S.,Lundback, T.,Ladenstein, R.,Hard, T. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat.Struct.Biol., 1:808-819, 1994 Cited by PubMed Abstract: The archaeon Sulfolobus solfataricus expresses large amounts of a small basic protein, Sso7d, which was previously identified as a DNA-binding protein possibly involved in compaction of DNA. We have determined the solution structure of Sso7d. The protein consists of a triple-stranded anti-parallel beta-sheet onto which an orthogonal double-stranded beta-sheet is packed. This topology is very similar to that found in eukaryotic Src homology-3 (SH3) domains. Sso7d binds strongly (Kd < 10 microM) to double-stranded DNA and protects it from thermal denaturation. In addition, we note that epsilon-mono-methylation of lysine side chains of Sso7d is governed by cell growth temperatures, suggesting that methylation is related to the heat-shock response. PubMed: 7634092DOI: 10.1038/nsb1194-808 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
