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PDBsum entry 3lnn

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protein metals Protein-protein interface(s) links
Metal transport PDB id
3lnn
Jmol
Contents
Protein chains
341 a.a. *
245 a.a. *
Metals
_ZN
Waters ×16
* Residue conservation analysis
PDB id:
3lnn
Name: Metal transport
Title: Crystal structure of zneb from cupriavidus metallidurans
Structure: Membrane fusion protein (mfp) heavy metal cation zneb (czcb-like). Chain: a, b. Synonym: secretion protein hlyd. Engineered: yes
Source: Cupriavidus metallidurans. Organism_taxid: 266264. Strain: ch34. Gene: rmet_5330, zneb. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.80Å     R-factor:   0.241     R-free:   0.314
Authors: J.K.Lee,F.De Angelis,L.J.Miercke,R.M.Stroud,G.Vandenbussche, For Structures Of Membrane Proteins (Csmp)
Key ref: F.De Angelis et al. (2010). Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc Natl Acad Sci U S A, 107, 11038-11043. PubMed id: 20534468
Date:
02-Feb-10     Release date:   30-Jun-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q1LCD7  (Q1LCD7_RALME) -  Membrane fusion protein (MFP-RND) heavy metal cation tricomponent efflux HmxB (CzcB-like)
Seq:
Struc:
385 a.a.
341 a.a.
Protein chain
Pfam   ArchSchema ?
Q1LCD7  (Q1LCD7_RALME) -  Membrane fusion protein (MFP-RND) heavy metal cation tricomponent efflux HmxB (CzcB-like)
Seq:
Struc:
385 a.a.
245 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     transmembrane transport   1 term 
  Biochemical function     metal ion binding     1 term  

 

 
Proc Natl Acad Sci U S A 107:11038-11043 (2010)
PubMed id: 20534468  
 
 
Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems.
F.De Angelis, J.K.Lee, J.D.O'Connell, L.J.Miercke, K.H.Verschueren, V.Srinivasan, C.Bauvois, C.Govaerts, R.A.Robbins, J.M.Ruysschaert, R.M.Stroud, G.Vandenbussche.
 
  ABSTRACT  
 
Resistance nodulation cell division (RND)-based efflux complexes mediate multidrug and heavy-metal resistance in many Gram-negative bacteria. Efflux of toxic compounds is driven by membrane proton/substrate antiporters (RND protein) in the plasma membrane, linked by a membrane fusion protein (MFP) to an outer-membrane protein. The three-component complex forms an efflux system that spans the entire cell envelope. The MFP is required for the assembly of this complex and is proposed to play an important active role in substrate efflux. To better understand the role of MFPs in RND-driven efflux systems, we chose ZneB, the MFP component of the ZneCAB heavy-metal efflux system from Cupriavidus metallidurans CH34. ZneB is shown to be highly specific for Zn(2+) alone. The crystal structure of ZneB to 2.8 A resolution defines the basis for metal ion binding in the coordination site at a flexible interface between the beta-barrel and membrane proximal domains. The conformational differences observed between the crystal structures of metal-bound and apo forms are monitored in solution by spectroscopy and chromatography. The structural rearrangements between the two states suggest an active role in substrate efflux through metal binding and release.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20981744 C.C.Su, F.Long, and E.W.Yu (2011).
The Cus efflux system removes toxic ions via a methionine shuttle.
  Protein Sci, 20, 6.  
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