1efz

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(New page: 200px<br /><applet load="1efz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efz, resolution 2.00&Aring;" /> '''MUTAGENESIS AND CRYS...)
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'''MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF ZYMOMONAS MOBILIS TRNA-GUANINE TRANSGLYCOSYLASE TO ELUCIDATE THE ROLE OF SERINE 103 FOR ENZYMATIC ACTIVITY'''<br />
'''MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF ZYMOMONAS MOBILIS TRNA-GUANINE TRANSGLYCOSYLASE TO ELUCIDATE THE ROLE OF SERINE 103 FOR ENZYMATIC ACTIVITY'''<br />
==Overview==
==Overview==
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The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved, in the exchange of guanine in the first position of the anticodon with, preQ1 as part of the biosynthesis of the hypermodified base queuine (Q)., Mutation of Ser90 to an alanine in Escherichia coli TGT leads to a, dramatic reduction of enzymatic activity (Reuter, K. et al. (1994), Biochemistry 33, 7041-7046). To further clarify the role of this residue, in the catalytic center, we have mutated the corresponding Ser103 of the, crystallizable Zymomonas mobilis TGT into alanine. The crystal structure, of a TGT(S103A)/preQ1 complex combined with biochemical data presented in, this paper suggest that Ser103 is essential for substrate orientation in, the TGT reaction.
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The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved in the exchange of guanine in the first position of the anticodon with preQ1 as part of the biosynthesis of the hypermodified base queuine (Q). Mutation of Ser90 to an alanine in Escherichia coli TGT leads to a dramatic reduction of enzymatic activity (Reuter, K. et al. (1994) Biochemistry 33, 7041-7046). To further clarify the role of this residue in the catalytic center, we have mutated the corresponding Ser103 of the crystallizable Zymomonas mobilis TGT into alanine. The crystal structure of a TGT(S103A)/preQ1 complex combined with biochemical data presented in this paper suggest that Ser103 is essential for substrate orientation in the TGT reaction.
==About this Structure==
==About this Structure==
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1EFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with ZN and PRF as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Queuine_tRNA-ribosyltransferase Queuine tRNA-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.29 2.4.2.29] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFZ OCA].
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1EFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zymomonas_mobilis Zymomonas mobilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PRF:'>PRF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Queuine_tRNA-ribosyltransferase Queuine tRNA-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.29 2.4.2.29] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFZ OCA].
==Reference==
==Reference==
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[[Category: Zymomonas mobilis]]
[[Category: Zymomonas mobilis]]
[[Category: Ficner, R.]]
[[Category: Ficner, R.]]
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[[Category: Garcia, G.A.]]
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[[Category: Garcia, G A.]]
[[Category: Gradler, U.]]
[[Category: Gradler, U.]]
[[Category: Klebe, G.]]
[[Category: Klebe, G.]]
[[Category: Reuter, K.]]
[[Category: Reuter, K.]]
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[[Category: Stubbs, M.T.]]
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[[Category: Stubbs, M T.]]
[[Category: PRF]]
[[Category: PRF]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: trna-modifying enzyme]]
[[Category: trna-modifying enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:58:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:27:20 2008''

Revision as of 10:27, 21 February 2008


1efz, resolution 2.00Å

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MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF ZYMOMONAS MOBILIS TRNA-GUANINE TRANSGLYCOSYLASE TO ELUCIDATE THE ROLE OF SERINE 103 FOR ENZYMATIC ACTIVITY

Overview

The tRNA modifying enzyme tRNA-guanine transglycosylase (TGT) is involved in the exchange of guanine in the first position of the anticodon with preQ1 as part of the biosynthesis of the hypermodified base queuine (Q). Mutation of Ser90 to an alanine in Escherichia coli TGT leads to a dramatic reduction of enzymatic activity (Reuter, K. et al. (1994) Biochemistry 33, 7041-7046). To further clarify the role of this residue in the catalytic center, we have mutated the corresponding Ser103 of the crystallizable Zymomonas mobilis TGT into alanine. The crystal structure of a TGT(S103A)/preQ1 complex combined with biochemical data presented in this paper suggest that Ser103 is essential for substrate orientation in the TGT reaction.

About this Structure

1EFZ is a Single protein structure of sequence from Zymomonas mobilis with and as ligands. Active as Queuine tRNA-ribosyltransferase, with EC number 2.4.2.29 Full crystallographic information is available from OCA.

Reference

Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity., Gradler U, Ficner R, Garcia GA, Stubbs MT, Klebe G, Reuter K, FEBS Lett. 1999 Jul 2;454(1-2):142-6. PMID:10413112

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