1sgv: Difference between revisions

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[[Image:1sgv.~~gif~~|left|200px]]

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

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~~'''~~STRUCTURE OF TRNA PSI55 PSEUDOURIDINE SYNTHASE (TRUB)~~'''~~

===STRUCTURE OF TRNA PSI55 PSEUDOURIDINE SYNTHASE (TRUB)===

~~==Overview==~~

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~~The three~~-~~dimensional structure of the RNA~~-~~modifying enzyme, psi55 tRNA pseudouridine synthase from Mycobacterium tuberculosis, is reported.~~ The ~~1.9-A resolution crystal structure reveals the enzyme~~, ~~free of substrate~~, ~~in two distinct conformations. The structure depicts an interesting mode of protein flexibility involving a hinged bending in~~ the ~~central beta-sheet of the catalytic module. Key parts of the active site cleft are also found~~ to ~~be disordered in~~ the ~~substrate-free form of the enzyme. The hinge bending~~ appears ~~to act as a clamp to position the substrate~~. ~~Our structural data furthers the previously proposed mechanism of tRNA recognition~~. ~~The present crystal structure emphasizes~~ the ~~significant role that protein dynamics must play in tRNA recognition, base flipping, and modification~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15028724}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15028724 is the PubMed ID number.

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==About this Structure==

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[[Category: Tbsgc]]

[[Category: Trna modification]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 08~~:41:18 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:50:31 2008''

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-[[Image:1sgv.gif|left|200px]]
+{{Seed}}
+[[Image:1sgv.png|left|200px]]
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 {{STRUCTURE_1sgv|  PDB=1sgv  |  SCENE=  }}
-'''STRUCTURE OF TRNA PSI55 PSEUDOURIDINE SYNTHASE (TRUB)'''
+===STRUCTURE OF TRNA PSI55 PSEUDOURIDINE SYNTHASE (TRUB)===
-==Overview==
+<!--
-The three-dimensional structure of the RNA-modifying enzyme, psi55 tRNA pseudouridine synthase from Mycobacterium tuberculosis, is reported. The 1.9-A resolution crystal structure reveals the enzyme, free of substrate, in two distinct conformations. The structure depicts an interesting mode of protein flexibility involving a hinged bending in the central beta-sheet of the catalytic module. Key parts of the active site cleft are also found to be disordered in the substrate-free form of the enzyme. The hinge bending appears to act as a clamp to position the substrate. Our structural data furthers the previously proposed mechanism of tRNA recognition. The present crystal structure emphasizes the significant role that protein dynamics must play in tRNA recognition, base flipping, and modification.
+The line below this paragraph, {{ABSTRACT_PUBMED_15028724}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15028724 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15028724}}
 ==About this Structure==
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 [[Category: Tbsgc]]
 [[Category: Trna modification]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:41:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:50:31 2008''