2z4h
From Proteopedia
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|PDB= 2z4h |SIZE=350|CAPTION= <scene name='initialview01'>2z4h</scene>, resolution 2.80Å | |PDB= 2z4h |SIZE=350|CAPTION= <scene name='initialview01'>2z4h</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= nlpE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= nlpE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2z4i|2Z4I]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z4h OCA], [http://www.ebi.ac.uk/pdbsum/2z4h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2z4h RCSB]</span> | ||
}} | }} | ||
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[[Category: Takeda, K.]] | [[Category: Takeda, K.]] | ||
[[Category: Tokuda, H.]] | [[Category: Tokuda, H.]] | ||
| - | [[Category: SO4]] | ||
[[Category: 3d domain swapping]] | [[Category: 3d domain swapping]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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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 Mon Mar 31 05:18:26 2008'' |
Revision as of 02:18, 31 March 2008
| |||||||
| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | nlpE (Escherichia coli) | ||||||
| Related: | 2Z4I
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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