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1j3l

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(New page: 200px<br /><applet load="1j3l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j3l, resolution 2.30&Aring;" /> '''Structure of the RNA...)
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[[Image:1j3l.gif|left|200px]]<br /><applet load="1j3l" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j3l.gif|left|200px]]<br /><applet load="1j3l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j3l, resolution 2.30&Aring;" />
caption="1j3l, resolution 2.30&Aring;" />
'''Structure of the RNA-processing inhibitor RraA from Thermus thermophilis'''<br />
'''Structure of the RNA-processing inhibitor RraA from Thermus thermophilis'''<br />
==Overview==
==Overview==
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The menG gene product, thought to catalyze the final methylation in, vitamin K(2) synthesis, has recently been shown to inhibit RNase E in, Eschericha coli. The structure of the protein, since renamed RraA, has, been solved to 2.3 A using the multiple-wavelength anomalous diffraction, method and selenomethionine-substituted protein from Thermus thermophilus., The six molecules in the asymmetric unit are arranged as two similar, trimers which have a degree of interaction, suggesting biological, significance. The fold does not support the postulated methylation, function. Genomic analysis, specifically a lack of an RNase E homologue in, cases where homologues to RraA exist, indicates that the function is still, obscure.
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The menG gene product, thought to catalyze the final methylation in vitamin K(2) synthesis, has recently been shown to inhibit RNase E in Eschericha coli. The structure of the protein, since renamed RraA, has been solved to 2.3 A using the multiple-wavelength anomalous diffraction method and selenomethionine-substituted protein from Thermus thermophilus. The six molecules in the asymmetric unit are arranged as two similar trimers which have a degree of interaction, suggesting biological significance. The fold does not support the postulated methylation function. Genomic analysis, specifically a lack of an RNase E homologue in cases where homologues to RraA exist, indicates that the function is still obscure.
==About this Structure==
==About this Structure==
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1J3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with MG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J3L OCA].
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1J3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3L OCA].
==Reference==
==Reference==
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Miyano, M.]]
[[Category: Miyano, M.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Rehse, P.H.]]
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[[Category: Rehse, P H.]]
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[[Category: Tahirov, T.H.]]
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[[Category: Tahirov, T H.]]
[[Category: CL]]
[[Category: CL]]
[[Category: MG]]
[[Category: MG]]
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[[Category: vitamine k2]]
[[Category: vitamine k2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:02:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:36 2008''

Revision as of 11:18, 21 February 2008

Image:1j3l.gif

1j3l, resolution 2.30Å

Drag the structure with the mouse to rotate

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

Overview

The menG gene product, thought to catalyze the final methylation in vitamin K(2) synthesis, has recently been shown to inhibit RNase E in Eschericha coli. The structure of the protein, since renamed RraA, has been solved to 2.3 A using the multiple-wavelength anomalous diffraction method and selenomethionine-substituted protein from Thermus thermophilus. The six molecules in the asymmetric unit are arranged as two similar trimers which have a degree of interaction, suggesting biological significance. The fold does not support the postulated methylation function. Genomic analysis, specifically a lack of an RNase E homologue in cases where homologues to RraA exist, indicates that the function is still obscure.

About this Structure

1J3L is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis., Rehse PH, Kuroishi C, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1997-2002. Epub, 2004 Oct 20. PMID:15502308

Page seeded by OCA on Thu Feb 21 13:18:36 2008

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