1osd: Difference between revisions

Revision as of 16:03, 29 July 2008

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File:1osd.png

Template:STRUCTURE 1osd

crystal structure of Oxidized MerP from Ralstonia metallidurans CH34crystal structure of Oxidized MerP from Ralstonia metallidurans CH34

Template:ABSTRACT PUBMED 15123428

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

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-'''crystal structure of Oxidized MerP from Ralstonia metallidurans CH34'''
+===crystal structure of Oxidized MerP from Ralstonia metallidurans CH34===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15123428}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15123428 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15123428}}
 ==About this Structure==
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 [[Category: Perisplasm]]
 [[Category: Structural genomic]]
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