1ILC

DNA Bending by an Adenine-Thymine Tract and Its Role in Gene Regulation.

Summary for 1ILC

• Entry DOI: 10.2210/pdb1ilc/pdb
• Descriptor: 5'-D(*AP*CP*CP*GP*AP*AP*TP*TP*CP*GP*GP*T)-3' (2 entities in total)
• Functional Keywords: b-dna double helix, dodecamer duplex, hpv e2 dna target, dna
• Total number of polymer chains: 6
• Total formula weight: 21974.42

Authors

Hizver, J.,Rozenberg, H.,Frolow, F.,Rabinovich, D.,Shakked, Z. (deposition date: 2001-05-08, release date: 2002-05-08, Last modification date: 2024-04-03)

Primary citation

Hizver, J.,Rozenberg, H.,Frolow, F.,Rabinovich, D.,Shakked, Z.
DNA bending by an adenine--thymine tract and its role in gene regulation.
Proc.Natl.Acad.Sci.USA, 98:8490-8495, 2001

PubMed Abstract: To gain insight into the structural basis of DNA bending by adenine-thymine tracts (A-tracts) and their role in DNA recognition by gene-regulatory proteins, we have determined the crystal structure of the high-affinity DNA target of the cancer-associated human papillomavirus E2 protein. The three independent B-DNA molecules of the crystal structure determined at 2.2-A resolution are examples of A-tract-containing helices where the global direction and magnitude of curvature are in accord with solution data, thereby providing insights, at the base pair level, into the mechanism of DNA bending by such sequence motifs. A comparative analysis of E2-DNA conformations with respect to other structural and biochemical studies demonstrates that (i) the A-tract structure of the core region, which is not contacted by the protein, is critical for the formation of the high-affinity sequence-specific protein-DNA complex, and (ii) differential binding affinity is regulated by the intrinsic structure and deformability encoded in the base sequence of the DNA target.

PubMed: 11438706
DOI: 10.1073/pnas.151247298

Experimental method

X-RAY DIFFRACTION (2.2 Å)