2d1u: Difference between revisions

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[[Image:2d1u.gif|left|200px]]<br /><applet load="2d1u" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2d1u.gif|left|200px]]<br /><applet load="2d1u" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2d1u" />

'''Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli'''<br />

==Overview==

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.

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.

==About this Structure==

2D1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA].

2D1U is a [http://en.wikipedia.org/wiki/Single_protein 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].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Garcia-Herrero, A.]]

[[Category: Vogel, H.J.]]

[[Category: Vogel, H J.]]

[[Category: feca]]

[[Category: iron-uptake]]

[[Category: surface signaling]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 09:23:~~39 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:33 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2d1u.gif|left|200px]]<br /><applet load="2d1u" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2d1u.gif|left|200px]]<br /><applet load="2d1u" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2d1u" />
 '''Solution strcuture of the periplasmic signaling domain of FecA from Escherichia coli'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-D1U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D1U OCA].
+D1U is a [http://en.wikipedia.org/wiki/Single_protein 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].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Garcia-Herrero, A.]]
-[[Category: Vogel, H.J.]]
+[[Category: Vogel, H J.]]
 [[Category: feca]]
 [[Category: iron-uptake]]
 [[Category: surface signaling]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:23:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:33 2008''