1kfo

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(New page: 200px<br /><applet load="1kfo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfo, resolution 1.60&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1kfo.gif|left|200px]]<br /><applet load="1kfo" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kfo, resolution 1.60&Aring;" />
caption="1kfo, resolution 1.60&Aring;" />
'''CRYSTAL STRUCTURE OF AN RNA HELIX RECOGNIZED BY A ZINC-FINGER PROTEIN: AN 18 BASE PAIR DUPLEX AT 1.6 RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF AN RNA HELIX RECOGNIZED BY A ZINC-FINGER PROTEIN: AN 18 BASE PAIR DUPLEX AT 1.6 RESOLUTION'''<br />
==Overview==
==Overview==
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The crystal structure of the 19-mer RNA, 5'-GAAUGCCUGCGAGCAUCCC-3' has, been determined from X-ray diffraction data to 1.6 A resolution by the, multiwavelength anomalous diffraction method from crystals containing a, brominated uridine. In the crystal, this RNA forms an 18-mer, self-complementary double helix with the 19th nucleotide flipped out of, the helix. This helix contains most of the target stem recognized by the, bacteriophage Mu Com protein (control of mom), which activates translation, of an unusual DNA modification enzyme, Mom. The 19-mer duplex, which, contains one A.C mismatch and one A.C/G.U tandem wobble pair, was shown to, bind to the Com protein by native gel electrophoresis shift assay., Comparison of the geometries and base stacking properties between, Watson-Crick base pairs and the mismatches in the crystal structure, suggest that both hydrogen bonding and base stacking are important for, stabilizing these mismatched base pairs, and that the unusual geometry, adopted by the A.C mismatch may reveal a unique structural motif required, for the function of Com.
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The crystal structure of the 19-mer RNA, 5'-GAAUGCCUGCGAGCAUCCC-3' has been determined from X-ray diffraction data to 1.6 A resolution by the multiwavelength anomalous diffraction method from crystals containing a brominated uridine. In the crystal, this RNA forms an 18-mer self-complementary double helix with the 19th nucleotide flipped out of the helix. This helix contains most of the target stem recognized by the bacteriophage Mu Com protein (control of mom), which activates translation of an unusual DNA modification enzyme, Mom. The 19-mer duplex, which contains one A.C mismatch and one A.C/G.U tandem wobble pair, was shown to bind to the Com protein by native gel electrophoresis shift assay. Comparison of the geometries and base stacking properties between Watson-Crick base pairs and the mismatches in the crystal structure suggest that both hydrogen bonding and base stacking are important for stabilizing these mismatched base pairs, and that the unusual geometry adopted by the A.C mismatch may reveal a unique structural motif required for the function of Com.
==About this Structure==
==About this Structure==
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1KFO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KFO OCA].
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1KFO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFO OCA].
==Reference==
==Reference==
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:16:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:37 2008''

Revision as of 11:33, 21 February 2008


1kfo, resolution 1.60Å

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CRYSTAL STRUCTURE OF AN RNA HELIX RECOGNIZED BY A ZINC-FINGER PROTEIN: AN 18 BASE PAIR DUPLEX AT 1.6 RESOLUTION

Overview

The crystal structure of the 19-mer RNA, 5'-GAAUGCCUGCGAGCAUCCC-3' has been determined from X-ray diffraction data to 1.6 A resolution by the multiwavelength anomalous diffraction method from crystals containing a brominated uridine. In the crystal, this RNA forms an 18-mer self-complementary double helix with the 19th nucleotide flipped out of the helix. This helix contains most of the target stem recognized by the bacteriophage Mu Com protein (control of mom), which activates translation of an unusual DNA modification enzyme, Mom. The 19-mer duplex, which contains one A.C mismatch and one A.C/G.U tandem wobble pair, was shown to bind to the Com protein by native gel electrophoresis shift assay. Comparison of the geometries and base stacking properties between Watson-Crick base pairs and the mismatches in the crystal structure suggest that both hydrogen bonding and base stacking are important for stabilizing these mismatched base pairs, and that the unusual geometry adopted by the A.C mismatch may reveal a unique structural motif required for the function of Com.

About this Structure

1KFO is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Crystal structure of an RNA helix recognized by a zinc-finger protein: an 18-bp duplex at 1.6 A resolution., Lima S, Hildenbrand J, Korostelev A, Hattman S, Li H, RNA. 2002 Jul;8(7):924-32. PMID:12166647

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