3fya

Crystal Structure of an R35A mutant of the Restriction-Modification Controller Protein C.Esp1396I

spinqualitylabelsall models 3fya, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fya is a 2 chain structure with sequence from Enterobacter sp. RFL1396. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GGH0_9ENTR 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 The controller protein of the Esp1396I restriction-modification (R-M) system binds differentially to three distinct operator sequences upstream of the methyltransferase (M) and endonuclease (R) genes to regulate the timing of gene expression. The crystal structure of a complex of the protein with two adjacent operator DNA sequences has been reported; however, the structure of the free protein has not yet been determined. Here, the crystal structure of the free protein is reported, with seven dimers in the asymmetric unit. Two of the 14 monomers show an alternative conformation to the major conformer in which the side chains of residues 43-46 in the loop region flanking the DNA-recognition helix are displaced by up to 10 A. It is proposed that the adoption of these two conformational states may play a role in DNA-sequence promiscuity. The two alternative conformations are also found in the R35A mutant structure, which is otherwise identical to the native protein. Comparison of the free and bound protein structures shows a 1.4 A displacement of the recognition helices when the dimer is bound to its DNA target. Structure of the restriction-modification controller protein C.Esp1396I.,Ball N, Streeter SD, Kneale GG, McGeehan JE Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):900-5. Epub 2009 Aug 6. PMID:19690367 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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