1reg

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(New page: 200px<br /><applet load="1reg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1reg, resolution 1.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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caption="1reg, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The translational regulator protein regA is encoded by the T4, bacteriophage and binds to a region of messenger RNA (mRNA) that includes, the initiator codon. RegA is unusual in that it represses the translation, of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The, crystal structure of regA was determined at 1.9 A resolution; the protein, was shown to have an alpha-helical core and two regions with antiparallel, beta sheets. One of these beta sheets has four antiparallel strands and, has some sequence homology to RNP-1 and RNP-2, which are believed to be, RNA-binding motifs and are found in a number of known RNA-binding, proteins. Structurally guided mutants may help to uncover the basis for, this variety of RNA interaction.
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The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.
==About this Structure==
==About this Structure==
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1REG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1REG OCA].
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1REG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REG OCA].
==Reference==
==Reference==
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[[Category: translational regulator protein]]
[[Category: translational regulator protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:31:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:02 2008''

Revision as of 12:50, 21 February 2008


1reg, resolution 1.9Å

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CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION

Overview

The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.

About this Structure

1REG is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.

Reference

Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution., Kang C, Chan R, Berger I, Lockshin C, Green L, Gold L, Rich A, Science. 1995 May 26;268(5214):1170-3. PMID:7761833

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