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== | ||
<StructureSection load='1osd' size='340' side='right' caption='[[1osd]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1osd' size='340' side='right'caption='[[1osd]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1osd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43123 Atcc 43123]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSD OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[1osd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43123 Atcc 43123]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OSD FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hqi|2hqi]], [[1afi|1afi]], [[1afj|1afj]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hqi|2hqi]], [[1afi|1afi]], [[1afj|1afj]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MerP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119219 ATCC 43123])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MerP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119219 ATCC 43123])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1osd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osd OCA], [http://pdbe.org/1osd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1osd RCSB], [http://www.ebi.ac.uk/pdbsum/1osd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1osd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43123]] | [[Category: Atcc 43123]] | ||
[[Category: Large Structures]] | |||
[[Category: Cohen-Addad, C]] | [[Category: Cohen-Addad, C]] | ||
[[Category: Coves, J]] | [[Category: Coves, J]] | ||
Revision as of 10:14, 9 December 2020
crystal structure of Oxidized MerP from Ralstonia metallidurans CH34crystal structure of Oxidized MerP from Ralstonia metallidurans CH34
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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