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PDBsum entry 2pub

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Transcription/DNA PDB id
2pub
Contents
Protein chain
338 a.a. *
DNA/RNA
Ligands
ADE
Waters ×53
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structure of laci member, Purr, Bound to DNA: minor groove binding by alpha helices.
Authors M.A.Schumacher, K.Y.Choi, H.Zalkin, R.G.Brennan.
Ref. Science, 1994, 266, 763-770. [DOI no: 10.1126/science.7973627]
PubMed id 7973627
Abstract
The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.
Secondary reference #1
Title Structure-Based redesign of corepressor specificity of the escherichia coli purine repressor by substitution of residue 190.
Authors F.Lu, M.A.Schumacher, D.N.Arvidson, A.Haldimann, B.L.Wanner, H.Zalkin, R.G.Brennan.
Ref. Biochemistry, 1998, 37, 971-982. [DOI no: 10.1021/bi971942s]
PubMed id 9454587
Full text Abstract
PROCHECK
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