Crystal Structure of the Oxidized Form of the Periplasmic Mercury-binding Protein MerP from Ralstonia metallidurans CH34

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 A...

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Veröffentlicht in:	Journal of molecular biology 2004-05, Vol.339 (1), p.161-171
Hauptverfasser:	Serre, Laurence, Rossy, Emmanuel, Pebay-Peyroula, Eva, Cohen-Addad, Claudine, Covès, Jacques
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Arabidopsis Proteins Carrier Proteins - chemistry chaperone Crystallization Escherichia coli - metabolism Membrane Proteins - chemistry Membrane Proteins - metabolism Mercury - metabolism mercury resistance metal binding metal trafficking Models, Molecular Molecular Chaperones Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction protein Protein Folding Protein Structure, Secondary Proteins - chemistry Proteins - metabolism Ralstonia - chemistry Ralstonia - metabolism Ralstonia metallidurans Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - chemistry Shigella flexneri Solutions Superoxide Dismutase - chemistry
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