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| | ==Crystal structure of the CusBA heavy-metal efflux complex from Escherichia coli== | | ==Crystal structure of the CusBA heavy-metal efflux complex from Escherichia coli== |
| | <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NE5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ne5]] is a 3 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), cusA, ybdE, b0575, JW0564 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusB, ylcD, b0574, JW0563 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), cusA, ybdE, b0575, JW0564 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ne5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne5 PDBsum]</span></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=3ne5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne5 OCA], [http://pdbe.org/3ne5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ne5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[http://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> [[http://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3ne5" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli k-12]] | + | [[Category: Ecoli]] |
| | [[Category: Su,C C]] | | [[Category: Su,C C]] |
| | [[Category: Metal transport]] | | [[Category: Metal transport]] |
| | [[Category: Transmembrane helix]] | | [[Category: Transmembrane helix]] |
| Structural highlights
3ne5 is a 3 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Gene: | cusB, ylcD, b0574, JW0563 (ECOLI), cusA, ybdE, b0575, JW0564 (ECOLI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CUSB_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver.[1] [2] [CUSA_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver.[3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem. 2001 Aug 17;276(33):30670-7. Epub 2001 Jun 8. PMID:11399769 doi:http://dx.doi.org/10.1074/jbc.M104122200
- ↑ Franke S, Grass G, Rensing C, Nies DH. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J Bacteriol. 2003 Jul;185(13):3804-12. PMID:12813074
- ↑ Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem. 2001 Aug 17;276(33):30670-7. Epub 2001 Jun 8. PMID:11399769 doi:http://dx.doi.org/10.1074/jbc.M104122200
- ↑ Franke S, Grass G, Rensing C, Nies DH. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J Bacteriol. 2003 Jul;185(13):3804-12. PMID:12813074
- ↑ Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, Yu EW. Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature. 2011 Feb 24;470(7335):558-62. PMID:21350490 doi:10.1038/nature09743
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