1pvr | pdb_00001pvr

BASIS FOR A SWITCH IN SUBSTRATE SPECIFICITY: CRYSTAL STRUCTURE OF SELECTED VARIANT OF CRE SITE-SPECIFIC RECOMBINASE, LNSGG BOUND TO THE LOXP (WILDTYPE) RECOGNITION SITE

spinqualitylabelsall models 1pvr, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pvr is a 4 chain structure with sequence from Bpp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1kbu, 1ma7, 1crx, 3crx, 4crx, 1nzb, 1ouq, 1f44, 1pvp, 1pvq Gene: CRE (BPP1) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RECR_BPP1] Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state. 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 basis for the altered DNA specificities of two Cre recombinase variants, obtained by mutation and selection, was revealed by their cocrystal structures. The proteins share similar substitutions but differ in their preferences for the natural LoxP substrate and an engineered substrate that is inactive with wild-type Cre, LoxM7. One variant preferentially recombines LoxM7 and contacts the substituted bases through a hydrated network of novel interlocking protein-DNA contacts. The other variant recognizes both LoxP and LoxM7 utilizing the same DNA backbone contact but different base contacts, facilitated by an unexpected DNA shift. Assisted by water, novel interaction networks can arise from few protein substitutions, suggesting how new DNA binding specificities might evolve. The contributions of macromolecular plasticity and water networks in specific DNA recognition observed here present a challenge for predictive schemes. A specificity switch in selected cre recombinase variants is mediated by macromolecular plasticity and water.,Baldwin EP, Martin SS, Abel J, Gelato KA, Kim H, Schultz PG, Santoro SW Chem Biol. 2003 Nov;10(11):1085-94. PMID:14652076 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Resolvase 3D structures

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