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4k7r

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Revision as of 07:20, 5 August 2016

Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation

Structural highlights

4k7r is a 1 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:	4k34, 4k7k
Gene:	b0572, cusC, ibeB, JW0561, ylcB (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CUSC_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.^[1] ^[2]

Publication Abstract from PubMed

Gram-negative bacteria, such as Escherichia coli, frequently utilize tripartite efflux complexes in the RND (resistance-nodulation-cell division) family to expel diverse toxic compounds from the cell. These complexes span both the inner and outer membranes of the bacterium via an alpha-helical, inner membrane transporter; a periplasmic membrane fusion protein; and a beta-barrel, outer membrane channel. One such efflux system, CusCBA, is responsible for extruding biocidal Cu(I) and Ag(I) ions. To remove these toxic ions, the CusC outer membrane channel must form a beta-barrel structural domain, which creates a pore and spans the entire outer membrane. We here report the crystal structures of wild-type CusC, as well as two CusC mutants, suggesting that the first N-terminal cysteine residue plays an important role in protein-membrane interactions and is critical for the insertion of this channel protein into the outer membrane. These structures provide insight into the mechanisms on CusC folding and transmembrane channel formation. It is also found that the interactions between CusC and membrane may be crucial for controlling the opening and closing of this beta-barrel, outer membrane channel.

Crystal Structures of CusC Review Conformational Changes Accompanying Folding and Transmembrane Channel Formation.,Lei HT, Bolla JR, Su CC, Yu EW J Mol Biol. 2013 Oct 4. pii: S0022-2836(13)00626-8. doi:, 10.1016/j.jmb.2013.09.042. PMID:24099674^[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
↑ Lei HT, Bolla JR, Su CC, Yu EW. Crystal Structures of CusC Review Conformational Changes Accompanying Folding and Transmembrane Channel Formation. J Mol Biol. 2013 Oct 4. pii: S0022-2836(13)00626-8. doi:, 10.1016/j.jmb.2013.09.042. PMID:24099674 doi:http://dx.doi.org/10.1016/j.jmb.2013.09.042

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k7r"

@@ Line 1: / Line 1: @@
 ==Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation==
 <StructureSection load='4k7r' size='340' side='right' caption='[[4k7r]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k34|4k34]], [[4k7k|4k7k]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0572, cusC, ibeB, JW0561, ylcB ([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=4k7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k7r RCSB], [http://www.ebi.ac.uk/pdbsum/4k7r 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=4k7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7r OCA], [http://pdbe.org/4k7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7r RCSB], [http://www.ebi.ac.uk/pdbsum/4k7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7r ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4k7r" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4k7r

From Proteopedia

Revision as of 07:20, 5 August 2016

Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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