2a02

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(New page: 200px<br /><applet load="2a02" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a02" /> '''Solution NMR Structure of the Periplasmic Si...)
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'''Solution NMR Structure of the Periplasmic Signaling Domain of the Outer Membrane Iron Transporter PupA from Pseudomonas putida.'''<br />
'''Solution NMR Structure of the Periplasmic Signaling Domain of the Outer Membrane Iron Transporter PupA from Pseudomonas putida.'''<br />
==Overview==
==Overview==
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Transcription of the ferric citrate import system is regulated by ferric, citrate binding to the outer membrane transporter FecA. A signal, indicating transporter occupancy is relayed across the outer membrane to, energy-transducing and regulatory proteins embedded in the cytoplasmic, membrane. Because transcriptional activation is not coupled to ferric, citrate import, an allosteric mechanism underlies this complex signaling, mechanism. Using evolution-based statistical analysis we have identified a, sparse but structurally connected network of residues that links distant, functional sites in FecA. Functional analyses of these positions confirm, their involvement in the mechanism that regulates transcriptional, activation in response to ferric citrate binding at the cell surface. This, mechanism appears to be conserved and provides the structural basis for, the allosteric signaling of TonB-dependent transporters.
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Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer membrane to energy-transducing and regulatory proteins embedded in the cytoplasmic membrane. Because transcriptional activation is not coupled to ferric citrate import, an allosteric mechanism underlies this complex signaling mechanism. Using evolution-based statistical analysis we have identified a sparse but structurally connected network of residues that links distant functional sites in FecA. Functional analyses of these positions confirm their involvement in the mechanism that regulates transcriptional activation in response to ferric citrate binding at the cell surface. This mechanism appears to be conserved and provides the structural basis for the allosteric signaling of TonB-dependent transporters.
==About this Structure==
==About this Structure==
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2A02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A02 OCA].
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2A02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A02 OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Amezcua, C.A.]]
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[[Category: Amezcua, C A.]]
[[Category: Chelliah, Y.]]
[[Category: Chelliah, Y.]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: Ferguson, A.D.]]
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[[Category: Ferguson, A D.]]
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[[Category: Rosen, M.K.]]
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[[Category: Rosen, M K.]]
[[Category: membrane protein]]
[[Category: membrane protein]]
[[Category: metal transport]]
[[Category: metal transport]]
[[Category: protein nmr]]
[[Category: protein nmr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:50:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:19 2008''

Revision as of 14:22, 21 February 2008


2a02

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Solution NMR Structure of the Periplasmic Signaling Domain of the Outer Membrane Iron Transporter PupA from Pseudomonas putida.

Overview

Transcription of the ferric citrate import system is regulated by ferric citrate binding to the outer membrane transporter FecA. A signal indicating transporter occupancy is relayed across the outer membrane to energy-transducing and regulatory proteins embedded in the cytoplasmic membrane. Because transcriptional activation is not coupled to ferric citrate import, an allosteric mechanism underlies this complex signaling mechanism. Using evolution-based statistical analysis we have identified a sparse but structurally connected network of residues that links distant functional sites in FecA. Functional analyses of these positions confirm their involvement in the mechanism that regulates transcriptional activation in response to ferric citrate binding at the cell surface. This mechanism appears to be conserved and provides the structural basis for the allosteric signaling of TonB-dependent transporters.

About this Structure

2A02 is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Signal transduction pathway of TonB-dependent transporters., Ferguson AD, Amezcua CA, Halabi NM, Chelliah Y, Rosen MK, Ranganathan R, Deisenhofer J, Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):513-8. Epub 2006 Dec 29. PMID:17197416

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