1G4D

NMR STRUCTURE OF THE MU BACTERIOPHAGE REPRESSOR DNA-BINDING DOMAIN/DNA COMPLEX

Summary for 1G4D

• Entry DOI: 10.2210/pdb1g4d/pdb
• Related: 1QPM
• Descriptor: 5'-D(P*CP*CP*TP*TP*TP*TP*CP*AP*GP*TP*AP*AP*TP*CP*TP*G)-3', 5'-D(P*CP*AP*GP*AP*TP*TP*AP*CP*TP*GP*AP*AP*AP*AP*GP*G)-3', REPRESSOR PROTEIN C (3 entities in total)
• Functional Keywords: protein-dna complex, helix-turn-helix, winged-helix, bacteriophage mu, repressor, virus/viral protein, viral protein-dna complex, viral protein/dna
• Biological source: Enterobacteria phage Mu
• Total number of polymer chains: 3
• Total formula weight: 17338.11

Authors

Wojciak, J.M.,Iwahara, J.,Clubb, R.T. (deposition date: 2000-10-26, release date: 2000-11-08, Last modification date: 2024-05-22)

Primary citation

Wojciak, J.M.,Iwahara, J.,Clubb, R.T.
The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove.
Nat.Struct.Biol., 8:84-90, 2001

PubMed Abstract: We have determined the solution structure of the complex between the 'winged-helix' enhancer binding domain of the Mu repressor protein and its cognate DNA site. The structure reveals an unusual use for the 'wing' which becomes immobilized upon DNA binding where it makes intermolecular hydrogen bond contacts deep within the minor groove. Although the wing is mobile in the absence of DNA, it partially negates the large entropic penalty associated with its burial by maintaining a small degree of structural order in the DNA-free state. Extensive contacts are also formed between the recognition helix and the DNA, which reads the major groove of a highly conserved region of the binding site through a single base-specific hydrogen bond and van der Waals contacts.

PubMed: 11135677
DOI: 10.1038/89582

Experimental method

SOLUTION NMR