Pseudouridine synthase: Difference between revisions

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(pseudo)uridine is a nucleoside, not nucleotide; other improvements in redaction
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The conversion of uridine to pseudouridine is accompanied by a conformational change of pseudouridine synthase<ref>PMID:14990747</ref>. <scene name='46/465439/Cv/3'>tRNA pseudouridine synthase binding with pseudouridine monophosphate</scene> ([[1ze2]]).  
The conversion of uridine to pseudouridine is accompanied by a conformational change of pseudouridine synthase<ref>PMID:14990747</ref>. <scene name='46/465439/Cv/3'>tRNA pseudouridine synthase binding with pseudouridine monophosphate</scene> ([[1ze2]]).  
</StructureSection>
</StructureSection>
== 3D Structures of deaminase ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* Pseudouridine synthase
**[[1dj0]] – EcPUS I – Escherichia coli<br />
**[[1ze1]] – TmPUS B – Thermotoga maritima<br />
**[[1ksk]], [[1ksl]] – EcPUS RsuA <br />
**[[1vio]] - PUS RsuA – Haemophilus influenzae<br />
**[[1xpi]] - EcPUS RluC catalytic domain<br />
**[[1v9k]] - EcPUS RluC C-terminal domain (mutant) <br />
**[[2ist]] - EcPUS RluD <br />
**[[1prz]], [[1qyu]], [[1v9f]] - EcPUS RluD catalytic domain<br />
**[[2olw]] - EcPUS RluE<br />
**[[2oml]] - EcPUS RluE catalytic domain<br />
**[[2gml]] - EcPUS RluF catalytic domain<br />
**[[4iqm]], [[4its]], [[4j37]], [[4nz6]] - hPUS Pus1 catalytic domain - human<br />
**[[4nz7]] - hPUS Pus1 catalytic domain (mutant)<br />
**[[1vs3]] – PUS TruA – Thermus thermophilus<br />
**[[1sgv]] – PUS TruB – Mycobacterium tuberculosis<br />
**[[1si7]], [[1szw]], [[1sb7]] - EcPUS TruD<br />
* Pseudouridine synthase complex with RNA
**[[1k8w]] – EcPUS B + stem-loop RNA <br />
**[[1zl3]] - EcPUS B (mutant) + stem-loop RNA<br />
**[[2i82]] – EcPUS RluA + RNA<br />
**[[3dh3]] - EcPUS RluF + RNA<br />
**[[2nqp]], [[2nr0]], [[2nre]] – EcPUS TruA + Leu-tRNA<br />
**[[3hjw]], [[3lwo]], [[3lwp]], [[3lwq]], [[3lwr]], [[3lwv]] – PfPUS Cbf5 + ribosome biogenesis protein Nop10 + ribosomal protein L7 + RNA – Pyrococcus furiosus<br />
**[[3mqk]] - PfPUS Cbf5 + ribosome biogenesis protein Nop10 + small nuclear RNP Gar1-like protein + RNA<br />
**[[3hjy]] - PfPUS Cbf5 + ribosome biogenesis protein NOP10 + RNA<br />
**[[1ze2]] - TmPUS B + RNA<br />
**[[2ab4]] - TmPUS B (mutant) + RNA<br />
**[[1r3e]], [[1r3f]] - EcPUS B + RNA<br />
* Probable pseudouridine synthase
**[[2apo]] – PPUS + ribosome biogenesis protein Nop10 – Methanocaldococcus jannaschii<br />
**[[2ey4]] - PfPPUS Cbf5 + ribosome biogenesis protein Nop10 + small nucleolar RNP <br />
**[[2hvy]], [[3hax]] - PfPPUS B + ribosome biogenesis protein Nop10 + ribosomal protein L7 + RNA<br />
**[[2rfk]] - PfPUS B + ribosome biogenesis protein Nop10 + small nucleolar RNP + RNA<br />
**[[3hay]] - PfPPUS B + ribosome biogenesis protein Nop10 + ribosomal protein L7 + small nucleolar RNP + RNA<br />
**[[2aus]] – PPUS B + ribosome biogenesis protein Nop10 – Pyrococcus abyssi
**[[1z2z]] – PPUS D – Methanosarcina mazei<br />
}}

Revision as of 12:43, 5 February 2019

Pseudouridine is an abundant modified nucleoside found in RNA molecules. It is formed post-transcriptionally in RNA molecules by isomerization of the bond between base and ribose in uridine. There are two major types of enzymes that catalyze this reaction:

  • RNA-guided pseudouridine synthase -- Some ribonucleoproteins (complexes of proteins and small RNAs) have been identified in archaea and eukaryotes to catalyze these reactions. The small RNA in the complex serves as a guide element to select the site of modification through base-pairing with the target RNA molecule.

Structural highlights

The conversion of uridine to pseudouridine is accompanied by a conformational change of pseudouridine synthase[1]. (1ze2).

tRNA pseudouridine synthase complex with RNA that contains pseudouridine monophosphate 1ze2

Drag the structure with the mouse to rotate

3D Structures of deaminase3D Structures of deaminase

Updated on 05-February-2019

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Wayne Decatur, Angel Herraez