1p6r

Solution structure of the DNA binding domain of the repressor BlaI.

spinqualitylabelsall models 1p6r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1p6r is a 1 chain structure with sequence from Bacillus licheniformis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLAI_BACLI Transcriptional repressor that constitutively blocks expression of beta-lactamase. Regulates genes involved in antibiotic resistance. Binds DNA as a dimer. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Two repressors (BlaI and MecI) regulate expression of these inducible proteins. Here, we present the first solution structure of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis BlaI which is very similar in primary sequence to the medically significant Staphyloccocal BlaI and MecI proteins. This structure is composed of a compact core of three alpha-helices and a three-stranded beta-sheet typical of the winged helix protein (WHP) family. The protein/DNA complex was studied by NMR chemical shift comparison between the free and complexed forms of BlaI. Residues involved in DNA interaction were identified and a WHP canonical model of interaction with the operators is proposed. In this model, specific contacts occur between the base-pairs of the TACA motif and conserved amino acid residues of the repressor helix H3. These results help toward understanding the repression and induction mechanism of the genes coding for beta-lactamase and PBP2'. Solution structural study of BlaI: implications for the repression of genes involved in beta-lactam antibiotic resistance.,Melckebeke HV, Vreuls C, Gans P, Filee P, Llabres G, Joris B, Simorre JP J Mol Biol. 2003 Oct 31;333(4):711-20. PMID:14568532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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