1C8C

CRYSTAL STRUCTURES OF THE CHROMOSOMAL PROTEINS SSO7D/SAC7D BOUND TO DNA CONTAINING T-G MISMATCHED BASE PAIRS

Summary for 1C8C

• Entry DOI: 10.2210/pdb1c8c/pdb
• NMR Information: BMRB: 5905,5908,5909,5910
• Descriptor: 5'-D(*GP*TP*GP*AP*TP*CP*GP*C)-3', DNA-BINDING PROTEIN 7A (3 entities in total)
• Functional Keywords: dna binding protein, protein-dna interaction, protein stability, hyperthermophile, achaeabacteria, electrostatics, molecular modeling, t-g mismatch, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm : P39476
• Total number of polymer chains: 3
• Total formula weight: 12121.80

Authors

Su, S.,Gao, Y.-G.,Robinson, H.,Liaw, Y.-C.,Edmondson, S.P.,Shriver, J.W.,Wang, A.H.-J. (deposition date: 2000-05-04, release date: 2001-05-04, Last modification date: 2023-08-09)

Primary citation

Su, S.,Gao, Y.G.,Robinson, H.,Liaw, Y.C.,Edmondson, S.P.,Shriver, J.W.,Wang, A.H.
Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.
J.Mol.Biol., 303:395-403, 2000

PubMed Abstract: Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation.

PubMed: 11031116
DOI: 10.1006/jmbi.2000.4112

Experimental method

X-RAY DIFFRACTION (1.45 Å)