1dj0: Difference between revisions

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[[Image:1dj0.~~jpg~~|left|200px]]

[[Image:1dj0.png|left|200px]]

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~~'''~~THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION~~'''~~

===THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION===

~~==Overview==~~

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~~Pseudouridine synthases catalyze the isomerization of specific uridines to pseudouridine in a variety of RNAs, yet the basis for recognition of the RNA sites or how they catalyze~~ this ~~reaction is unknown. The crystal structure of pseudouridine synthase I from Escherichia coli~~, ~~which~~, ~~for example, modifies positions 38, 39 and/or 40 in tRNA, reveals a dimeric protein that contains two positively charged, RNA-binding clefts along~~ the ~~surface of~~ the ~~protein~~. ~~Each cleft contains a highly conserved aspartic acid located at its center~~. ~~The structural domains have a topological similarity to those of other RNA-binding proteins~~, ~~though~~ the ~~mode of interaction with tRNA appears to be unique. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10625422}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10625422 is the PubMed ID number.

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==About this Structure==

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[[Category: Rna-binding motif]]

[[Category: Rna-modifying enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:54:03 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:08:20 2008''

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-[[Image:1dj0.jpg|left|200px]]
+{{Seed}}
+[[Image:1dj0.png|left|200px]]
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 {{STRUCTURE_1dj0|  PDB=1dj0  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION'''
+===THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION===
-==Overview==
+<!--
-Pseudouridine synthases catalyze the isomerization of specific uridines to pseudouridine in a variety of RNAs, yet the basis for recognition of the RNA sites or how they catalyze this reaction is unknown. The crystal structure of pseudouridine synthase I from Escherichia coli, which, for example, modifies positions 38, 39 and/or 40 in tRNA, reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved aspartic acid located at its center. The structural domains have a topological similarity to those of other RNA-binding proteins, though the mode of interaction with tRNA appears to be unique. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation.
+The line below this paragraph, {{ABSTRACT_PUBMED_10625422}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10625422 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10625422}}
 ==About this Structure==
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 [[Category: Rna-binding motif]]
 [[Category: Rna-modifying enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:54:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:08:20 2008''