Summary information and primary citation

PDB-id
1oct; DSSR-derived features in text and JSON formats
Class
transcription-DNA
Method
X-ray (3.0 Å)
Summary
Crystal structure of the oct-1 pou domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
Reference
Klemm, J.D., Rould, M.A., Aurora, R., Herr, W., Pabo, C.O.: (1994) "Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules." Cell, 77, 21-32.
Abstract
The structure of an Oct-1 POU domain-octamer DNA complex has been solved at 3.0 A resolution. The POU-specific domain contacts the 5' half of this site (ATGCAAAT), and as predicted from nuclear magnetic resonance studies, the structure, docking, and contacts are remarkably similar to those of the lambda and 434 repressors. The POU homeodomain contacts the 3' half of this site (ATGCAAAT), and the docking is similar to that of the engrailed, MAT alpha 2, and Antennapedia homeodomains. The linker region is not visible and there are no protein-protein contacts between the domains, but overlapping phosphate contacts near the center of the octamer site may favor cooperative binding. This novel arrangement raises important questions about cooperativity in protein-DNA recognition.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js