2z4h
From Proteopedia
Crystal structure of the Cpx pathway activator NlpE from Escherichia coli
Structural highlights
FunctionNLPE_ECOLI Involved in copper homeostasis. Could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes. When overproduced induces degP through the activation of the two-component system CpxA/CpxR.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNlpE, 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. Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.,Hirano Y, Hossain MM, Takeda K, Tokuda H, Miki K Structure. 2007 Aug;15(8):963-76. PMID:17698001[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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