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1j3l
From Proteopedia
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|PDB= 1j3l |SIZE=350|CAPTION= <scene name='initialview01'>1j3l</scene>, resolution 2.30Å | |PDB= 1j3l |SIZE=350|CAPTION= <scene name='initialview01'>1j3l</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3l OCA], [http://www.ebi.ac.uk/pdbsum/1j3l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j3l RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Rehse, P H.]] | [[Category: Rehse, P H.]] | ||
[[Category: Tahirov, T H.]] | [[Category: Tahirov, T H.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: MG]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| Line 33: | Line 34: | ||
[[Category: vitamine k2]] | [[Category: vitamine k2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:23 2008'' |
Revision as of 18:28, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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