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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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Revision as of 19:52, 29 October 2007

Image:2bti.gif

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]. 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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