1prz: Difference between revisions
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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=" | [[Image:1prz.jpg|left|200px]]<br /><applet load="1prz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1prz, resolution 1.80Å" /> | caption="1prz, resolution 1.80Å" /> | ||
'''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 | 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:// | 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 | [[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]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:57 2008'' | ||