1BF4
CHROMOSOMAL DNA-BINDING PROTEIN SSO7D/D(GCGAACGC) COMPLEX
Summary for 1BF4
Entry DOI | 10.2210/pdb1bf4/pdb |
NMR Information | BMRB: 5909,5910 |
Descriptor | DNA (5'-D(*GP*CP*GP*TP*5IUP*CP*GP*C)-3'), DNA (5'-D(*GP*CP*GP*AP*AP*CP*GP*C)-3'), PROTEIN (CHROMOSOMAL PROTEIN SSO7D), ... (4 entities in total) |
Functional Keywords | dna binding protein, hyperthermophile, archaebacteria, complex (dna-binding protein-dna), dna-binding protein-dna complex, dna-binding protein/dna |
Biological source | Sulfolobus acidocaldarius |
Cellular location | Cytoplasm : P13123 |
Total number of polymer chains | 3 |
Total formula weight | 12131.47 |
Authors | Su, S.,Gao, Y.-G.,Robinson, H.,Padmanabhan, S.,Lim, L.,Shriver, J.W.,Wang, A.H.-J. (deposition date: 1998-05-27, release date: 1999-11-10, Last modification date: 2024-04-03) |
Primary citation | Gao, Y.G.,Su, S.Y.,Robinson, H.,Padmanabhan, S.,Lim, L.,McCrary, B.S.,Edmondson, S.P.,Shriver, J.W.,Wang, A.H. The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA. Nat.Struct.Biol., 5:782-786, 1998 Cited by PubMed Abstract: Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing. PubMed: 9731772DOI: 10.1038/1822 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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