1y00

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(New page: 200px<br /><applet load="1y00" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y00" /> '''Solution structure of the Carbon Storage Reg...)
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[[Image:1y00.gif|left|200px]]<br /><applet load="1y00" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y00.gif|left|200px]]<br /><applet load="1y00" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of the Carbon Storage Regulator protein CsrA'''<br />
'''Solution structure of the Carbon Storage Regulator protein CsrA'''<br />
==Overview==
==Overview==
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The carbon storage regulator A (CsrA) is a protein responsible for the, repression of a variety of stationary-phase genes in bacteria. In this, work, we describe the nuclear magnetic resonance (NMR)-based structure of, the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two, identical subunits, each composed of five strands, a small alpha-helix and, a flexible C terminus. NMR titration experiments suggest that the, beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important, elements in RNA binding. Even though the beta3-beta4 loop contains a, highly conserved RNA-binding motif, GxxG, typical of KH domains, our, structure excludes CsrA from being a member of this protein family, as, previously suggested. A mechanism for the recognition of mRNAs, downregulated by CsrA is proposed.
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The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small alpha-helix and a flexible C terminus. NMR titration experiments suggest that the beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important elements in RNA binding. Even though the beta3-beta4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.
==About this Structure==
==About this Structure==
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1Y00 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=1Y00 OCA].
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1Y00 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=1Y00 OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Gehring, K.]]
[[Category: Gehring, K.]]
[[Category: Gutierrez, P.]]
[[Category: Gutierrez, P.]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]
[[Category: Liu, Q.]]
[[Category: Liu, Q.]]
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[[Category: Osborne, M.J.]]
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[[Category: Osborne, M J.]]
[[Category: bsgi]]
[[Category: bsgi]]
[[Category: carbon storage regulation]]
[[Category: carbon storage regulation]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:28:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:25 2008''

Revision as of 14:00, 21 February 2008


1y00

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Solution structure of the Carbon Storage Regulator protein CsrA

Overview

The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small alpha-helix and a flexible C terminus. NMR titration experiments suggest that the beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important elements in RNA binding. Even though the beta3-beta4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.

About this Structure

1Y00 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Solution structure of the carbon storage regulator protein CsrA from Escherichia coli., Gutierrez P, Li Y, Osborne MJ, Pomerantseva E, Liu Q, Gehring K, J Bacteriol. 2005 May;187(10):3496-501. PMID:15866937

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