1yy3
From Proteopedia
(New page: 200px<br /><applet load="1yy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yy3, resolution 2.88Å" /> '''Structure of S-Adeno...) |
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| - | [[Image:1yy3.gif|left|200px]]<br /><applet load="1yy3" size=" | + | [[Image:1yy3.gif|left|200px]]<br /><applet load="1yy3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yy3, resolution 2.88Å" /> | caption="1yy3, resolution 2.88Å" /> | ||
'''Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)'''<br /> | '''Structure of S-Adenosylmethionine:tRNA Ribosyltransferase-Isomerase (QueA)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The enzyme S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) | + | 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== | ==About this Structure== | ||
| - | 1YY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1YY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YY3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trna-modification]] | [[Category: trna-modification]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:18 2008'' |
Revision as of 14:10, 21 February 2008
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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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