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1j3l

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{{STRUCTURE_1j3l| PDB=1j3l | SCENE= }}
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'''Structure of the RNA-processing inhibitor RraA from Thermus thermophilis'''
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===Structure of the RNA-processing inhibitor RraA from Thermus thermophilis===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 15502308 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15502308}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Vitamine k2]]
[[Category: Vitamine k2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:45:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:27:10 2008''

Revision as of 11:27, 1 July 2008

Image:1j3l.png

Template:STRUCTURE 1j3l

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

Template:ABSTRACT PUBMED 15502308

About this Structure

1J3L is a Single protein structure of sequence from Thermus thermophilus. 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 Tue Jul 1 14:27:10 2008

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