From Proteopedia
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| - | [[Image:2d1u.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2d1u.png|left|200px]] |
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| | {{STRUCTURE_2d1u| PDB=2d1u | SCENE= }} | | {{STRUCTURE_2d1u| PDB=2d1u | SCENE= }} |
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| - | '''Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli'''
| + | ===Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli=== |
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| - | ==Overview==
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| - | Gram-negative bacteria possess outer membrane receptors that utilize energy provided by the TonB system to take up iron. Several of these receptors participate in extracytoplasmic factor (ECF) signalling through an N-terminal signalling domain that interacts with a periplasmic transmembrane anti-sigma factor protein and a cytoplasmic sigma factor protein. The structures of the intact TonB-dependent outer membrane receptor FecA from Escherichia coli and FpvA from Pseudomonas aeruginosa have recently been solved by protein crystallography; however, no electron density was detected for their periplasmic signalling domains, suggesting that it was either unfolded or flexible with respect to the remainder of the protein. Here we describe the well-defined solution structure of this domain solved by multidimensional nuclear magnetic resonance (NMR) spectroscopy. The monomeric protein construct contains the 79-residue N-terminal domain as well as the next 17 residues that are part of the receptor's plug domain. These form two clearly distinct regions: a highly structured domain at the N-terminal end followed by an extended flexible tail at the C-terminal end, which includes the 'TonB-box' region, and connects it to the plug domain of the receptor. The structured region consists of two alpha-helices that are positioned side by side and are sandwiched in between two small beta-sheets. This is a novel protein fold which appears to be preserved in all the periplasmic signalling domains of bacterial TonB-dependent outer membrane receptors that are involved in ECF signalling, because the hydrophobic residues that make up the core of the protein domain are highly conserved.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16313612}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16313612 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16313612}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2D1U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA]. | + | 2D1U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Iron-uptake]] | | [[Category: Iron-uptake]] |
| | [[Category: Surface signaling]] | | [[Category: Surface signaling]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:32:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:54:02 2008'' |
Revision as of 09:54, 29 July 2008
Template:STRUCTURE 2d1u
Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli
Template:ABSTRACT PUBMED 16313612
About this Structure
2D1U is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli., Garcia-Herrero A, Vogel HJ, Mol Microbiol. 2005 Dec;58(5):1226-37. PMID:16313612
Page seeded by OCA on Tue Jul 29 12:54:02 2008
