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2d1u

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[[Image:2d1u.gif|left|200px]]
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{{Seed}}
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[[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'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16313612 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16313612}}
==About this Structure==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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[[Category: Iron-uptake]]
[[Category: Iron-uptake]]
[[Category: Surface signaling]]
[[Category: Surface signaling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:32:08 2008''
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''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

Image:2d1u.png

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

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