1AZP
HYPERTHERMOPHILE CHROMOSOMAL PROTEIN SAC7D BOUND WITH KINKED DNA DUPLEX
Summary for 1AZP
Entry DOI | 10.2210/pdb1azp/pdb |
NMR Information | BMRB: 5905,5908 |
Descriptor | DNA (5'-D(*GP*CP*GP*AP*TP*CP*GP*C)-3'), PROTEIN (HYPERTHERMOPHILE CHROMOSOMAL PROTEIN SAC7D) (3 entities in total) |
Functional Keywords | complex (chromatin protein-dna), dna-binding, archea kinked-dna, minor-groove binding, intercalation, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Sulfolobus acidocaldarius |
Total number of polymer chains | 3 |
Total formula weight | 12482.12 |
Authors | Robinson, H.,Gao, Y.-G.,Mccrary, B.S.,Edmondson, S.P.,Shriver, J.W.,Wang, A.H.-J. (deposition date: 1997-11-19, release date: 1999-01-13, Last modification date: 2024-02-07) |
Primary citation | Robinson, H.,Gao, Y.G.,McCrary, B.S.,Edmondson, S.P.,Shriver, J.W.,Wang, A.H. The hyperthermophile chromosomal protein Sac7d sharply kinks DNA. Nature, 392:202-205, 1998 Cited by PubMed Abstract: The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution. PubMed: 9515968DOI: 10.1038/32455 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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