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1AZP

HYPERTHERMOPHILE CHROMOSOMAL PROTEIN SAC7D BOUND WITH KINKED DNA DUPLEX

Summary for 1AZP
Entry DOI10.2210/pdb1azp/pdb
NMR InformationBMRB: 5905,5908
DescriptorDNA (5'-D(*GP*CP*GP*AP*TP*CP*GP*C)-3'), PROTEIN (HYPERTHERMOPHILE CHROMOSOMAL PROTEIN SAC7D) (3 entities in total)
Functional Keywordscomplex (chromatin protein-dna), dna-binding, archea kinked-dna, minor-groove binding, intercalation, dna binding protein-dna complex, dna binding protein/dna
Biological sourceSulfolobus acidocaldarius
Total number of polymer chains3
Total formula weight12482.12
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 citationRobinson, 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: 9515968
DOI: 10.1038/32455
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

226707

數據於2024-10-30公開中

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