title: Crystal structure of the oxidized form of the periplasmic mercury-binding protein MerP from Ralstonia metallidurans CH34.
abstract: In Ralstonia metallidurans CH34, the gene merP encodes for a periplasmic mercury-binding protein which is capable of binding one mercury atom. The metal-binding site of MerP consists of the highly conserved sequence GMTCXXC found in the family that includes metallochaperones and metal-transporting ATPases. We purified MerP from R.metallidurans CH34 and solved its crystal structure under the oxidized form at 2.0A resolution. Superposition with structures of other metal-binding proteins shows that the global structure of R.metallidurans CH34 oxidized MerP follows the general topology of the whole family. The largest differences are observed with the NMR structure of oxidized Shigella flexneri MerP. Detailed analysis of the metal-binding site suggests a direct role for Y66 in stabilizing the thiolate group of C17 during the mercury-binding reaction. The metal-binding site of oxidized MerP is also similar to the metal-binding sites of oxidized copper chaperone for superoxide dismutase and Atx1, two copper-binding proteins from Saccharomyces cerevisiae. Finally, the packing of the MerP crystals suggests that F38, a well-conserved residue in the MerP family may be important in mercury binding and transfer. We propose a possible mechanism of mercury transfer between two CXXC motifs based on a transient bi-coordinated mercury intermediate.
authors.affiliation: Institut de Biologie Structurale, UMR 5075-CNRS-CEA-UJF/ IBS-LPM, 41 Avenue Jules Horowitz, 38027 Grenoble Cedex 01, France. laurence.serre@ibs.fr
authors.forename: Laurence
authors.initials: L
authors.lastname: Serre
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Rossy
authors.forename: Eva
authors.initials: E
authors.lastname: Pebay-Peyroula
authors.forename: Claudine
authors.initials: C
authors.lastname: Cohen-Addad
authors.forename: Jacques
authors.initials: J
authors.lastname: Covès
mesh_terms: D020816:Amino Acid Motifs; D029681:Arabidopsis Proteins; D002352:Carrier Proteins / Q000737:chemistry; D003460:Crystallization; D004926:Escherichia coli / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008628:Mercury / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D043367:Ralstonia / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D012996:Solutions; D013482:Superoxide Dismutase / Q000737:chemistry
chemical_list: C093341:ATX1 protein, S cerevisiae; D029681:Arabidopsis Proteins; C433183:CCH protein, Arabidopsis; D002352:Carrier Proteins; D008565:Membrane Proteins; C086060:MerP protein, Bacteria; D018832:Molecular Chaperones; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions; D013482:Superoxide Dismutase; D008628:Mercury