1yy3
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yy3 OCA], [http://www.ebi.ac.uk/pdbsum/1yy3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yy3 RCSB]</span> | ||
}} | }} | ||
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[[Category: trna-modification]] | [[Category: trna-modification]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:26:15 2008'' |
Revision as of 22:26, 30 March 2008
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| , resolution 2.88Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)
Overview
The enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) is involved in the biosynthesis of the hypermodified tRNA nucleoside queuosine. It is unprecedented in nature as it uses the cofactor S-adenosylmethionine as the donor of a ribosyl group. We have determined the crystal structure of Bacillus subtilis QueA at a resolution of 2.9A. The structure reveals two domains representing a 6-stranded beta-barrel and an alpha beta alpha-sandwich, respectively. All amino acid residues invariant in the QueA enzymes of known sequence cluster at the interface of the two domains indicating the localization of the substrate binding region and active center. Comparison of the B. subtilis QueA structure with the structure of QueA from Thermotoga maritima suggests a high domain flexibility of this enzyme.
About this Structure
1YY3 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase., Grimm C, Ficner R, Sgraja T, Haebel P, Klebe G, Reuter K, Biochem Biophys Res Commun. 2006 Dec 22;351(3):695-701. Epub 2006 Oct 30. PMID:17083917
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