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New page: left|200px<br /><applet load="1dj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dj0, resolution 1.50Å" /> '''THE CRYSTAL STRUCTUR...
 
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[[Image:1dj0.jpg|left|200px]]<br /><applet load="1dj0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dj0.jpg|left|200px]]<br /><applet load="1dj0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dj0, resolution 1.50&Aring;" />
caption="1dj0, resolution 1.50&Aring;" />
'''THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION'''<br />
'''THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION'''<br />


==Overview==
==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.
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.


==About this Structure==
==About this Structure==
1DJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DJ0 OCA].  
1DJ0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pseudouridylate_synthase Pseudouridylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.70 4.2.1.70] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJ0 OCA].  


==Reference==
==Reference==
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[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Foster, P.G.]]
[[Category: Foster, P G.]]
[[Category: Huang, L.]]
[[Category: Huang, L.]]
[[Category: Santi, D.V.]]
[[Category: Santi, D V.]]
[[Category: Stroud, R.M.]]
[[Category: Stroud, R M.]]
[[Category: CL]]
[[Category: CL]]
[[Category: alpha/beta fold]]
[[Category: alpha/beta fold]]
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[[Category: rna-modifying enzyme]]
[[Category: rna-modifying enzyme]]


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