1efz: Difference between revisions

Line 1:

[[Image:1efz.~~jpg~~|left|200px]]

[[Image:1efz.png|left|200px]]

<!--

Line 9:

Line 10:

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

===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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10413112}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10413112 is the PubMed ID number.

-->

==About this Structure==

Line 32:

Line 36:

[[Category: Transferase]]

[[Category: Trna-modifying enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:03:02 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:38:21 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1efz.jpg|left|200px]]
+{{Seed}}
+[[Image:1efz.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1efz|  PDB=1efz  |  SCENE=  }}
-'''MUTAGENESIS AND CRYSTALLOGRAPHIC STUDIES OF ZYMOMONAS MOBILIS TRNA-GUANINE TRANSGLYCOSYLASE TO ELUCIDATE THE ROLE OF SERINE 103 FOR ENZYMATIC ACTIVITY'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10413112}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10413112 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10413112}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Transferase]]
 [[Category: Trna-modifying enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:03:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:38:21 2008''