1YY3

Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)

Summary for 1YY3

• Entry DOI: 10.2210/pdb1yy3/pdb
• Descriptor: S-adenosylmethionine:tRNA ribosyltransferase-isomerase (1 entity in total)
• Functional Keywords: beta-barrel, quea, bacillus subtilis, quein queuosine, s-adenosylmethionine:trna ribosyltransferase-isomerase, trna-modification, isomerase
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (By similarity): O32054
• Total number of polymer chains: 2
• Total formula weight: 77680.08

Authors

Grimm, C.,Ficner, R.,Reuter, K. (deposition date: 2005-02-23, release date: 2006-03-21, Last modification date: 2024-03-13)

Primary citation

Grimm, C.,Ficner, R.,Sgraja, T.,Haebel, P.,Klebe, G.,Reuter, K.
Crystal structure of Bacillus subtilis S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Biochem.Biophys.Res.Commun., 351:695-701, 2006

PubMed Abstract: 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.

PubMed: 17083917
DOI: 10.1016/j.bbrc.2006.10.096

Experimental method

X-RAY DIFFRACTION (2.88 Å)