2d45
From Proteopedia
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Crystal structure of the MecI-mecA repressor-operator complex
Overview
The dimeric repressor MecI regulates the mecA gene that encodes the, penicillin-binding protein PBP-2a in methicillin-resistant Staphylococcus, aureus (MRSA). MecI is similar to BlaI, the repressor for the blaZ gene of, beta-lactamase. MecI and BlaI can bind to both operator DNA sequences. The, crystal structure of MecI in complex with the 32 base-pair cognate DNA of, mec was determined to 3.8 A resolution. MecI is a homodimer and each, monomer consists of a compact N-terminal winged-helix domain, which binds, to DNA, and a loosely packed C-terminal helical domain, which intertwines, with its counter-monomer. The crystal contains horizontal layers of, virtual DNA double helices extending in three directions, which are, separated by perpendicular DNA segments. Each DNA segment is bound to two, MecI dimers. Similar to the BlaI-mec complex, but unlike the MecI-bla, complex, the MecI repressors bind to both sides of the mec DNA dyad that, contains four conserved sequences of TACA/TGTA. The results confirm the, up-and-down binding to the mec operator, which may account for cooperative, effect of the repressor.
About this Structure
2D45 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structure of the MecI repressor from Staphylococcus aureus in complex with the cognate DNA operator of mec., Safo MK, Ko TP, Musayev FN, Zhao Q, Wang AH, Archer GL, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):320-4. Epub 2006 Mar 25. PMID:16582476
Page seeded by OCA on Wed Nov 21 09:26:04 2007
