1zeq

<StructureSection load='1zeq' size='340' side='right' caption='[[1zeq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1zeq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZEQ FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusF, cusX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zeq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zeq RCSB], [http://www.ebi.ac.uk/pdbsum/1zeq PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CUSF_ECOLI CUSF_ECOLI]] Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.<ref>PMID:11399769</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/1zeq_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

We have determined the crystal structure of apo-CusF, a periplasmic protein involved in copper and silver resistance in Escherichia coli. The protein forms a five-stranded beta-barrel, classified as an OB-fold, which is a unique topology for a copper-binding protein. NMR chemical shift mapping experiments suggest that Cu(I) is bound by conserved residues H36, M47, and M49 located in beta-strands 2 and 3. These residues are clustered at one end of the beta-barrel, and their side chains are oriented toward the interior of the barrel. Cu(I) can be modeled into the apo-CusF structure with only minimal structural changes using H36, M47, and M49 as ligands. The unique structure and metal binding site of CusF are distinct from those of previously characterized copper-binding proteins.

A novel copper-binding fold for the periplasmic copper resistance protein CusF.,Loftin IR, Franke S, Roberts SA, Weichsel A, Heroux A, Montfort WR, Rensing C, McEvoy MM Biochemistry. 2005 Aug 9;44(31):10533-40. PMID:16060662<ref>PMID:16060662</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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[[Category: Franke, S]]

[[Category: Heroux, A]]

[[Category: Loftin, I R]]

[[Category: McEvoy, M M]]

[[Category: Montfort, W R]]

[[Category: Rensing, C]]

[[Category: Roberts, S A]]

[[Category: Weichsel, A]]

[[Category: Ob-fold]]