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| | ==Crystal structures of the extrusion state of the CusBA adaptor-transporter complex== | | ==Crystal structures of the extrusion state of the CusBA adaptor-transporter complex== |
| - | <StructureSection load='3t53' size='340' side='right' caption='[[3t53]], [[Resolution|resolution]] 3.37Å' scene=''> | + | <StructureSection load='3t53' size='340' side='right'caption='[[3t53]], [[Resolution|resolution]] 3.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3t53]] 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=3T53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T53 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3t53]] 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=3T53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T53 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t51|3t51]], [[3t56|3t56]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3t51|3t51]], [[3t56|3t56]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0574, cusB, JW0563, ylcD ([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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0574, cusB, JW0563, ylcD ([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> |
| - | <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=3t53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t53 OCA], [http://pdbe.org/3t53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t53 RCSB], [http://www.ebi.ac.uk/pdbsum/3t53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t53 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=3t53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t53 OCA], [https://pdbe.org/3t53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t53 RCSB], [https://www.ebi.ac.uk/pdbsum/3t53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t53 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [[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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Long, F]] | | [[Category: Long, F]] |
| | [[Category: Su, C C]] | | [[Category: Su, C C]] |
| Structural highlights
3t53 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.
| | Ligands: | |
| Related: | |
| Gene: | b0574, cusB, JW0563, ylcD (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 expel various toxic chemicals via tripartite efflux pumps belonging to the resistance-nodulation-cell division superfamily. These pumps span both the inner and outer membranes of the cell. The three components of these tripartite systems are an inner-membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (or adaptor); and an outer-membrane-anchored channel. These three efflux proteins interact in the periplasmic space to form the three-part complexes. We previously presented the crystal structures of both the inner-membrane transporter CusA and membrane fusion protein CusB of the CusCBA tripartite efflux system from Escherichia coli. We also described the co-crystal structure of the CusBA adaptor-transporter, revealing that the trimeric CusA efflux pump assembles with six CusB protein molecules to form the complex CusB(6)-CusA(3). We here report three different conformers of the crystal structures of CusBA-Cu(I), suggesting a mechanism on how Cu(I) binding initiates a sequence of conformational transitions in the transport cycle. Genetic analysis and transport assays indicate that charged residues, in addition to the methionine pairs and clusters, are essential for extruding metal ions out of the cell.
Charged Amino Acids (R83, E567, D617, E625, R669, and K678) of CusA Are Required for Metal Ion Transport in the Cus Efflux System.,Su CC, Long F, Lei HT, Bolla JR, Do SV, Rajashankar KR, Yu EW J Mol Biol. 2012 Jun 6. PMID:22683351[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, Lei HT, Bolla JR, Do SV, Rajashankar KR, Yu EW. Charged Amino Acids (R83, E567, D617, E625, R669, and K678) of CusA Are Required for Metal Ion Transport in the Cus Efflux System. J Mol Biol. 2012 Jun 6. PMID:22683351 doi:10.1016/j.jmb.2012.05.038
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