1afi: Difference between revisions
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< | ==STRUCTURE OF THE REDUCED FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES== | ||
<StructureSection load='1afi' size='340' side='right'caption='[[1afi]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1afi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AFI FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afi OCA], [https://pdbe.org/1afi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afi RCSB], [https://www.ebi.ac.uk/pdbsum/1afi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afi ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MERP_SHIFL MERP_SHIFL] Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (MerA) via the MerT protein. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/1afi_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1afi ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria carrying plasmids with the mer operon, which encodes the proteins responsible for the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell membrane into the cytoplasm where it is reduced to Hg(0). This is significant because metallic mercury is relatively nontoxic and volatile and thus can be passively eliminated. The structures of the reduced and mercury-bound forms of merP, the periplasmic protein, which binds Hg(II) and transfers it to the membrane transport protein merT, have been determined in aqueous solution by multidimensional NMR spectroscopy. The 72-residue merP protein has a betaalpha betabeta alphabeta fold with the two alpha helices overlaying a four-strand antiparallel beta sheet. Structural differences between the reduced and mercury-bound forms of merP are localized to the metal binding loop containing the consensus sequence GMTCXXC. The structure of the mercury-bound form of merP shows that Hg(II) is bicoordinate with the Cys side chain ligands, and this is confirmed by the chemical shift frequency of the 199Hg resonance. | |||
Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.,Steele RA, Opella SJ Biochemistry. 1997 Jun 10;36(23):6885-95. PMID:9188683<ref>PMID:9188683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1afi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Opella | [[Category: Opella SJ]] | ||
[[Category: Steele | [[Category: Steele RA]] | ||
Latest revision as of 11:13, 22 May 2024
STRUCTURE OF THE REDUCED FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURESSTRUCTURE OF THE REDUCED FORM OF MERP, THE PERIPLASMIC PROTEIN FROM THE BACTERIAL MERCURY DETOXIFICATION SYSTEM, NMR, 20 STRUCTURES
Structural highlights
FunctionMERP_SHIFL Mercury scavenger that specifically binds to one mercury ion and which passes it to the mercuric reductase (MerA) via the MerT protein. 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 PubMedBacteria carrying plasmids with the mer operon, which encodes the proteins responsible for the bacterial mercury detoxification system, have the ability to transport Hg(II) across the cell membrane into the cytoplasm where it is reduced to Hg(0). This is significant because metallic mercury is relatively nontoxic and volatile and thus can be passively eliminated. The structures of the reduced and mercury-bound forms of merP, the periplasmic protein, which binds Hg(II) and transfers it to the membrane transport protein merT, have been determined in aqueous solution by multidimensional NMR spectroscopy. The 72-residue merP protein has a betaalpha betabeta alphabeta fold with the two alpha helices overlaying a four-strand antiparallel beta sheet. Structural differences between the reduced and mercury-bound forms of merP are localized to the metal binding loop containing the consensus sequence GMTCXXC. The structure of the mercury-bound form of merP shows that Hg(II) is bicoordinate with the Cys side chain ligands, and this is confirmed by the chemical shift frequency of the 199Hg resonance. Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.,Steele RA, Opella SJ Biochemistry. 1997 Jun 10;36(23):6885-95. PMID:9188683[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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