2z4h
From Proteopedia
(New page: 200px<br /><applet load="2z4h" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z4h, resolution 2.80Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | NlpE, an outer membrane lipoprotein, functions during envelope stress | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hirano, Y.]] | [[Category: Hirano, Y.]] | ||
| - | [[Category: Hossain, M | + | [[Category: Hossain, M M.]] |
[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Takeda, K.]] | [[Category: Takeda, K.]] | ||
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[[Category: signaling protein activator]] | [[Category: signaling protein activator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:00:06 2008'' |
Revision as of 17:00, 21 February 2008
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Crystal structure of the Cpx pathway activator NlpE from Escherichia coli
Overview
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.
About this Structure
2Z4H is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
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
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