2O97

Crystal Structure of E. coli HU heterodimer

Summary for 2O97

• Entry DOI: 10.2210/pdb2o97/pdb
• Descriptor: DNA-binding protein HU-alpha, DNA-binding protein HU-beta, NICKEL (II) ION, ... (5 entities in total)
• Functional Keywords: dna-binding, heterodimer, dna structure, dna supercoiling, e. coli, dna binding protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm, nucleoid : P0ACF0
• Total number of polymer chains: 2
• Total formula weight: 18883.70

Authors

Guo, F.,Adhya, S. (deposition date: 2006-12-13, release date: 2007-03-06, Last modification date: 2023-12-27)

Primary citation

Guo, F.,Adhya, S.
Spiral structure of Escherichia coli HU{alpha}beta provides foundation for DNA supercoiling.
Proc.Natl.Acad.Sci.Usa, 104:4309-4314, 2007

PubMed Abstract: We determined the crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein by x-ray diffraction and observed that the heterodimers form multimers with octameric units in three potential arrangements, which may serve specialized roles in different DNA transaction reactions. It is of special importance that one of the structures forms spiral filaments with left-handed rotations. A negatively superhelical DNA can be modeled to wrap around this left-handed HUalphabeta multimer. Whereas the wild-type HU generated negative DNA supercoiling in vitro, an engineered heterodimer with an altered amino acid residue critical for the formation of the left-handed spiral protein in the crystal was defective in the process, thus providing the structural explanation for the classical property of HU to restrain negative supercoils in DNA.

PubMed: 17360520
DOI: 10.1073/pnas.0611686104

Experimental method

X-RAY DIFFRACTION (2.45 Å)