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2Z4H

Crystal structure of the Cpx pathway activator NlpE from Escherichia coli

Summary for 2Z4H
Entry DOI10.2210/pdb2z4h/pdb
Related2Z4I
DescriptorCopper homeostasis protein cutF, SULFATE ION (2 entities in total)
Functional Keywordsouter memblane lipoprotein, beta barrel, ob-fold, 3d domain swapping, signaling protein activator
Biological sourceEscherichia coli
Cellular locationCell outer membrane; Lipid-anchor: P40710
Total number of polymer chains2
Total formula weight51371.30
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 citationHirano, 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: 17698001
DOI: 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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