|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the membrane fusion protein CusB from Escherichia coli.== | | ==Crystal structure of the membrane fusion protein CusB from Escherichia coli.== |
| - | <StructureSection load='3ow7' size='340' side='right' caption='[[3ow7]], [[Resolution|resolution]] 3.78Å' scene=''> | + | <StructureSection load='3ow7' size='340' side='right'caption='[[3ow7]], [[Resolution|resolution]] 3.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ow7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h9t 3h9t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OW7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ow7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h9t 3h9t]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OW7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ooc|3ooc]], [[3opo|3opo]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ooc|3ooc]], [[3opo|3opo]]</div></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])</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])</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=3ow7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ow7 OCA], [http://pdbe.org/3ow7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ow7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ow7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ow7 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=3ow7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ow7 OCA], [https://pdbe.org/3ow7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ow7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ow7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ow7 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> | + | [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 25: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Ecoli]] | | [[Category: Ecoli]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Su, C C]] | | [[Category: Su, C C]] |
| | [[Category: Beta barrel]] | | [[Category: Beta barrel]] |
| Structural highlights
Function
[CUSB_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver.[1] [2]
Publication Abstract from PubMed
Gram-negative bacteria, such as Escherichia coli, frequently utilize tripartite efflux complexes belonging to the resistance-nodulation-division family to expel diverse toxic compounds from the cell. These systems contain a periplasmic membrane fusion protein (MFP) that is critical for substrate transport. We here present the x-ray structures of the CusB MFP from the copper/silver efflux system of E. coli. This is the first structure of any MFPs associated with heavy-metal efflux transporters. CusB bridges the inner-membrane efflux pump CusA and outer-membrane channel CusC to mediate resistance to Cu(+) and Ag(+) ions. Two distinct structures of the elongated molecules of CusB were found in the asymmetric unit of a single crystal, which suggests the flexible nature of this protein. Each protomer of CusB can be divided into four different domains, whereby the first three domains are mostly beta-strands and the last domain adopts an entirely helical architecture. Unlike other known structures of MFPs, the alpha-helical domain of CusB is folded into a three-helix bundle. This three-helix bundle presumably interacts with the periplasmic domain of CusC. The N- and C-termini of CusB form the first beta-strand domain, which is found to interact with the periplasmic domain of the CusA efflux pump. Atomic details of how this efflux protein binds Cu(+) and Ag(+) were revealed by the crystals of the CusB-Cu(I) and CusB-Ag(I) complexes. The structures indicate that CusB consists of multiple binding sites for these metal ions. These findings reveal novel structural features of an MFP in the resistance-nodulation-division efflux system and provide direct evidence that this protein specifically interacts with transported substrates.
Crystal structure of the membrane fusion protein CusB from Escherichia coli.,Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK, Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW J Mol Biol. 2009 Oct 23;393(2):342-55. Epub 2009 Aug 18. PMID:19695261[3]
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
- ↑ Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK, Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, Yu EW. Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol. 2009 Oct 23;393(2):342-55. Epub 2009 Aug 18. PMID:19695261 doi:10.1016/j.jmb.2009.08.029
|
