1v2x: Difference between revisions

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[[Image:1v2x.~~jpg~~|left|200px]]

[[Image:1v2x.png|left|200px]]

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~~'''~~TrmH~~'''~~

===TrmH===

~~==Overview==~~

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The ~~tRNA(Gm18) methyltransferase (TrmH) catalyzes~~ the ~~2'-O methylation of guanosine 18~~ (~~Gua18) of tRNA. We solved the crystal structure of Thermus thermophilus TrmH complexed with S-adenosyl-L-methionine~~ at 1.~~85 A resolution~~. ~~The catalytic domain contains a deep trefoil knot, which mutational analyses revealed to be crucial for the formation of the catalytic site and the cofactor binding pocket. The tRNA dihydrouridine(D~~)~~-arm can be docked onto the dimeric TrmH~~, ~~so that the tRNA D-stem~~ is ~~clamped by~~ the N- ~~and C~~-terminal helices from one subunit while the Gua18 is modified by the other subunit. Arg41 from the other subunit enters the catalytic site and forms a hydrogen bond with a bound sulfate ion, an RNA main chain phosphate analog, thus activating its nucleophilic state. Based on Gua18 modeling onto the active site, we propose that once Gua18 binds, the phosphate group activates Arg41, which then deprotonates the 2'-OH group for methylation.

The line below this paragraph, {{ABSTRACT_PUBMED_15062082}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15062082 is the PubMed ID number.

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==About this Structure==

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[[Category: Rsgi]]

[[Category: Structural genomic]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 12~~:00:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:00:20 2008''

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-[[Image:1v2x.jpg|left|200px]]
+{{Seed}}
+[[Image:1v2x.png|left|200px]]
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 {{STRUCTURE_1v2x|  PDB=1v2x  |  SCENE=  }}
-'''TrmH'''
+===TrmH===
-==Overview==
+<!--
-The tRNA(Gm18) methyltransferase (TrmH) catalyzes the 2'-O methylation of guanosine 18 (Gua18) of tRNA. We solved the crystal structure of Thermus thermophilus TrmH complexed with S-adenosyl-L-methionine at 1.85 A resolution. The catalytic domain contains a deep trefoil knot, which mutational analyses revealed to be crucial for the formation of the catalytic site and the cofactor binding pocket. The tRNA dihydrouridine(D)-arm can be docked onto the dimeric TrmH, so that the tRNA D-stem is clamped by the N- and C-terminal helices from one subunit while the Gua18 is modified by the other subunit. Arg41 from the other subunit enters the catalytic site and forms a hydrogen bond with a bound sulfate ion, an RNA main chain phosphate analog, thus activating its nucleophilic state. Based on Gua18 modeling onto the active site, we propose that once Gua18 binds, the phosphate group activates Arg41, which then deprotonates the 2'-OH group for methylation.
+The line below this paragraph, {{ABSTRACT_PUBMED_15062082}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15062082 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15062082}}
 ==About this Structure==
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 [[Category: Rsgi]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:00:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:00:20 2008''