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2bti

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(New page: 200px<br /> <applet load="2bti" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bti, resolution 2.00&Aring;" /> '''STRUCTURE-FUNCTION ...)
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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 SO4 and ACT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTI OCA]].
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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 SO4 and ACT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTI OCA]].
==Reference==
==Reference==
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[[Category: rna binding protein]]
[[Category: rna binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:56:40 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:23:10 2007''

Revision as of 12:18, 30 October 2007


2bti, resolution 2.00Å

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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, ... [(full description)]

About this Structure

2BTI is a [Single protein] structure of sequence from [Yersinia enterocolitica] with SO4 and ACT as [ligands]. Structure known Active Site: AC1. 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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