2Z4H
Crystal structure of the Cpx pathway activator NlpE from Escherichia coli
Summary for 2Z4H
Entry DOI | 10.2210/pdb2z4h/pdb |
Related | 2Z4I |
Descriptor | Copper homeostasis protein cutF, SULFATE ION (2 entities in total) |
Functional Keywords | outer memblane lipoprotein, beta barrel, ob-fold, 3d domain swapping, signaling protein activator |
Biological source | Escherichia coli |
Cellular location | Cell outer membrane; Lipid-anchor: P40710 |
Total number of polymer chains | 2 |
Total formula weight | 51371.30 |
Authors | Hirano, Y.,Hossain, M.M.,Takeda, K.,Tokuda, H.,Miki, K. (deposition date: 2007-06-18, release date: 2007-09-04, Last modification date: 2021-11-10) |
Primary citation | Hirano, Y.,Hossain, M.M.,Takeda, K.,Tokuda, H.,Miki, K. Structural Studies of the Cpx Pathway Activator NlpE on the Outer Membrane of Escherichia coli Structure, 15:963-976, 2007 Cited by PubMed Abstract: NlpE, an outer membrane lipoprotein, functions during envelope stress responses in Gram-negative bacteria. In Escherichia coli, adhesion to abiotic surfaces has been reported to activate the Cpx pathway in an NlpE-dependent manner. External copper ions are also thought to activate the Cpx pathway mediated by NlpE. We determined the crystal structure of NlpE from E. coli at 2.6 A resolution. The structure showed that NlpE consists of two beta barrel domains. The N-terminal domain resembles the bacterial lipocalin Blc, and the C-terminal domain has an oligonucleotide/oligosaccharide-binding (OB) fold. From both biochemical analyses and the crystal structure, it can be deduced that the cysteine residues in the CXXC motif may be chemically active. Furthermore, two monomers in the asymmetric unit form an unusual 3D domain-swapped dimer. These findings indicate that tertiary and/or quaternary structural instability may be responsible for Cpx pathway activation. PubMed: 17698001DOI: 10.1016/j.str.2007.06.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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