1osd: Difference between revisions
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'''crystal structure of Oxidized MerP from Ralstonia metallidurans CH34''' | '''crystal structure of Oxidized MerP from Ralstonia metallidurans CH34''' | ||
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[[Category: Rossy, E.]] | [[Category: Rossy, E.]] | ||
[[Category: Serre, L.]] | [[Category: Serre, L.]] | ||
[[Category: | [[Category: Mercury resistance]] | ||
[[Category: | [[Category: Metal binding protein]] | ||
[[Category: | [[Category: Perisplasm]] | ||
[[Category: | [[Category: Structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:13:39 2008'' | |||
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Revision as of 04:13, 3 May 2008
crystal structure of Oxidized MerP from Ralstonia metallidurans CH34
OverviewOverview
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.
About this StructureAbout this Structure
1OSD is a Single protein structure of sequence from Cupriavidus metallidurans. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the oxidized form of the periplasmic mercury-binding protein MerP from Ralstonia metallidurans CH34., Serre L, Rossy E, Pebay-Peyroula E, Cohen-Addad C, Coves J, J Mol Biol. 2004 May 21;339(1):161-71. PMID:15123428 Page seeded by OCA on Sat May 3 04:13:39 2008