1PVP

BASIS FOR A SWITCH IN SUBSTRATE SPECIFICITY: CRYSTAL STRUCTURE OF SELECTED VARIANT OF CRE SITE-SPECIFIC RECOMBINASE, ALSHG BOUND TO THE ENGINEERED RECOGNITION SITE LOXM7

Summary for 1PVP

• Entry DOI: 10.2210/pdb1pvp/pdb
• Related: 1CRX 1F44 1KBU 1MA7 1NZB 1OUQ 1PVQ 1PVR 3CRX 4CRX
• Descriptor: 34-MER, Recombinase cre, ... (4 entities in total)
• Functional Keywords: cre, recombinase, dna, cre-loxp recombination, recombination-dna complex, recombination/dna
• Biological source: Escherichia phage P1 (Bacteriophage P1); More
• Total number of polymer chains: 4
• Total formula weight: 99430.33

Authors

Baldwin, E.P.,Martin, S.S.,Abel, J.,Gelato, K.A.,Kim, H.,Schultz, P.G.,Santoro, S.W. (deposition date: 2003-06-28, release date: 2004-02-17, Last modification date: 2023-08-16)

Primary citation

Baldwin, E.P.,Martin, S.S.,Abel, J.,Gelato, K.A.,Kim, H.,Schultz, P.G.,Santoro, S.W.
A specificity switch in selected cre recombinase variants is mediated by macromolecular plasticity and water.
Chem.Biol., 10:1085-1094, 2003

PubMed Abstract: 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.

PubMed: 14652076
DOI: 10.1016/j.chembiol.2003.10.015

Experimental method

X-RAY DIFFRACTION (2.35 Å)