2bti

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[[Image:2bti.gif|left|200px]]<br /><applet load="2bti" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bti.gif|left|200px]]
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caption="2bti, resolution 2.00&Aring;" />
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'''STRUCTURE-FUNCTION STUDIES OF THE RMSA CSRA POST-TRANSCRIPTIONAL GLOBAL REGULATOR PROTEIN FAMILY REVEALS A CLASS OF RNA-BINDING STRUCTURE'''<br />
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{{Structure
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|PDB= 2bti |SIZE=350|CAPTION= <scene name='initialview01'>2bti</scene>, resolution 2.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE-FUNCTION STUDIES OF THE RMSA CSRA POST-TRANSCRIPTIONAL GLOBAL REGULATOR PROTEIN FAMILY REVEALS A CLASS OF RNA-BINDING STRUCTURE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BTI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTI OCA].
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2BTI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTI OCA].
==Reference==
==Reference==
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Functional analysis of the post-transcriptional regulator RsmA reveals a novel RNA-binding site., Heeb S, Kuehne SA, Bycroft M, Crivii S, Allen MD, Haas D, Camara M, Williams P, J Mol Biol. 2006 Feb 3;355(5):1026-36. Epub 2005 Dec 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16359708 16359708]
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Functional analysis of the post-transcriptional regulator RsmA reveals a novel RNA-binding site., Heeb S, Kuehne SA, Bycroft M, Crivii S, Allen MD, Haas D, Camara M, Williams P, J Mol Biol. 2006 Feb 3;355(5):1026-36. Epub 2005 Dec 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16359708 16359708]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia enterocolitica]]
[[Category: Yersinia enterocolitica]]
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[[Category: rna binding protein]]
[[Category: rna binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:35 2008''

Revision as of 14:06, 20 March 2008

Image:2bti.gif


PDB ID 2bti

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE-FUNCTION STUDIES OF THE RMSA CSRA POST-TRANSCRIPTIONAL GLOBAL REGULATOR PROTEIN FAMILY REVEALS A CLASS OF RNA-BINDING STRUCTURE


Overview

The RsmA family of RNA-binding proteins are global post-transcriptional regulators that mediate extensive changes in gene expression in bacteria. They bind to, and affect the translation rate of target mRNAs, a function that is further modulated by one or more, small, untranslated competitive regulatory RNAs. To gain new insights into the nature of this protein/RNA interaction, we used X-ray crystallography to solve the structure of the Yersinia enterocolitica RsmA homologue. RsmA consists of a dimeric beta barrel from which two alpha helices are projected. From structure-based alignments of the RsmA protein family from diverse bacteria, we identified key amino acid residues likely to be involved in RNA-binding. Site-specific mutagenesis revealed that arginine at position 44, located at the N terminus of the alpha helix is essential for biological activity in vivo and RNA-binding in vitro. Mutation of this site affects swarming motility, exoenzyme and secondary metabolite production in the human pathogen Pseudomonas aeruginosa, carbon metabolism in Escherichia coli, and hydrogen cyanide production in the plant beneficial strain Pseudomonas fluorescens CHA0. R44A mutants are also unable to interact with the small untranslated RNA, RsmZ. Thus, although possessing a motif similar to the KH domain of some eukaryotic RNA-binding proteins, RsmA differs substantially and incorporates a novel class of RNA-binding site.

About this Structure

2BTI is a Single protein structure of sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA.

Reference

Functional analysis of the post-transcriptional regulator RsmA reveals a novel RNA-binding site., Heeb S, Kuehne SA, Bycroft M, Crivii S, Allen MD, Haas D, Camara M, Williams P, J Mol Biol. 2006 Feb 3;355(5):1026-36. Epub 2005 Dec 1. PMID:16359708

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