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| | <StructureSection load='3ne5' size='340' side='right'caption='[[3ne5]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='3ne5' size='340' side='right'caption='[[3ne5]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ne5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NE5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ne5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NE5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusB, ylcD, b0574, JW0563 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), cusA, ybdE, b0575, JW0564 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.898Å</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=3ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne5 OCA], [https://pdbe.org/3ne5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ne5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ne5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne5 ProSAT]</span></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=3ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne5 OCA], [https://pdbe.org/3ne5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ne5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ne5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CUSB_ECOLI CUSB_ECOLI]] Part of a cation efflux system that mediates resistance to copper and silver.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref> [[https://www.uniprot.org/uniprot/CUSA_ECOLI CUSA_ECOLI]] Part of a cation efflux system that mediates resistance to copper and silver.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref>
| + | [https://www.uniprot.org/uniprot/CUSB_ECOLI CUSB_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Gram-negative bacteria, such as Escherichia coli, expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membrane. The three parts are an inner membrane, substrate-binding transporter; a membrane fusion protein; and an outer-membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. A crystallographic model of this tripartite efflux complex has been unavailable because co-crystallization of the various components of the system has proven to be extremely difficult. We previously described the crystal structures of both the inner membrane transporter CusA and the membrane fusion protein CusB of the CusCBA efflux system of E. coli. Here we report the co-crystal structure of the CusBA efflux complex, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. The six CusB molecules seem to form a continuous channel. The affinity of the CusA and CusB interaction was found to be in the micromolar range. Finally, we have predicted a three-dimensional structure for the trimeric CusC outer membrane channel and developed a model of the tripartite efflux assemblage. This CusC(3)-CusB(6)-CusA(3) model shows a 750-kilodalton efflux complex that spans the entire bacterial cell envelope and exports Cu I and Ag I ions.
| + | |
| - | | + | |
| - | Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.,Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, Yu EW Nature. 2011 Feb 24;470(7335):558-62. PMID:21350490<ref>PMID:21350490</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3ne5" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Su, C C]] | + | [[Category: Su C-C]] |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Transmembrane helix]]
| + | |
