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New page: left|200px<br /><applet load="1prz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prz, resolution 1.80Å" /> '''Crystal structure of...
 
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[[Image:1prz.jpg|left|200px]]<br /><applet load="1prz" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1prz.jpg|left|200px]]<br /><applet load="1prz" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1prz, resolution 1.80&Aring;" />
caption="1prz, resolution 1.80&Aring;" />
'''Crystal structure of pseudouridine synthase RluD catalytic module'''<br />
'''Crystal structure of pseudouridine synthase RluD catalytic module'''<br />


==Overview==
==Overview==
Pseudouridine (5-beta-D-ribofuranosyluracil, Psi) is the most commonly, found modified base in RNA. Conversion of uridine to Psi is performed, enzymatically in both prokaryotes and eukaryotes by pseudouridine, synthases (EC 4.2.1.70). The Escherichia coli Psi-synthase RluD modifies, uridine to Psi at positions 1911, 1915 and 1917 within 23S rRNA. RluD also, possesses a second function related to proper assembly of the 50S, ribosomal subunit that is independent of Psi-synthesis. Here, we report, the crystal structure of the catalytic module of RluD (residues 68-326;, DeltaRluD) refined at 1.8A to a final R-factor of 21.8% (R(free)=24.3%)., DeltaRluD is a monomeric enzyme having an overall mixed alpha/beta fold., The DeltaRluD molecule consists of two subdomains, a catalytic subdomain, and C-terminal subdomain with the RNA-binding cleft formed by loops, extending from the catalytic sub-domain. The catalytic sub-domain of, DeltaRluD has a similar fold as in TruA, TruB and RsuA, with the location, of the RNA-binding cleft, active-site and conserved, catalytic Asp residue, superposing in all four structures. Superposition of the crystal structure, of TruB bound to a T-stem loop with RluD reveals that similar RNA-protein, interactions for the flipped-out uridine base would exist in both, structures, implying that base-flipping is necessary for catalysis. This, observation also implies that the specificity determinants for, site-specific RNA-binding and recognition likely reside in parts of RluD, beyond the active site.
Pseudouridine (5-beta-D-ribofuranosyluracil, Psi) is the most commonly found modified base in RNA. Conversion of uridine to Psi is performed enzymatically in both prokaryotes and eukaryotes by pseudouridine synthases (EC 4.2.1.70). The Escherichia coli Psi-synthase RluD modifies uridine to Psi at positions 1911, 1915 and 1917 within 23S rRNA. RluD also possesses a second function related to proper assembly of the 50S ribosomal subunit that is independent of Psi-synthesis. Here, we report the crystal structure of the catalytic module of RluD (residues 68-326; DeltaRluD) refined at 1.8A to a final R-factor of 21.8% (R(free)=24.3%). DeltaRluD is a monomeric enzyme having an overall mixed alpha/beta fold. The DeltaRluD molecule consists of two subdomains, a catalytic subdomain and C-terminal subdomain with the RNA-binding cleft formed by loops extending from the catalytic sub-domain. The catalytic sub-domain of DeltaRluD has a similar fold as in TruA, TruB and RsuA, with the location of the RNA-binding cleft, active-site and conserved, catalytic Asp residue superposing in all four structures. Superposition of the crystal structure of TruB bound to a T-stem loop with RluD reveals that similar RNA-protein interactions for the flipped-out uridine base would exist in both structures, implying that base-flipping is necessary for catalysis. This observation also implies that the specificity determinants for site-specific RNA-binding and recognition likely reside in parts of RluD beyond the active site.


==About this Structure==
==About this Structure==
1PRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1PRZ OCA].  
1PRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1PRZ OCA].  


==Reference==
==Reference==
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[[Category: Pseudouridylate synthase]]
[[Category: Pseudouridylate synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Cygler, M.]]
[[Category: Cygler, M.]]
[[Category: Iannuzzi, P.]]
[[Category: Iannuzzi, P.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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