5bth

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==Crystal structure of Candida albicans Rai1==
==Crystal structure of Candida albicans Rai1==
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<StructureSection load='5bth' size='340' side='right' caption='[[5bth]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='5bth' size='340' side='right'caption='[[5bth]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5bth]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BTH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5bth]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BTH FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5btb|5btb]], [[5bte|5bte]], [[5bto|5bto]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bth OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bth RCSB], [http://www.ebi.ac.uk/pdbsum/5bth PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bth OCA], [https://pdbe.org/5bth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bth RCSB], [https://www.ebi.ac.uk/pdbsum/5bth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bth ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DXO_CANAL DXO_CANAL]] Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping and pyrophosphohydrolase activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates (By similarity).
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[https://www.uniprot.org/uniprot/DXO_CANAL DXO_CANAL] Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping and pyrophosphohydrolase activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Recent studies showed that Rai1 and its homologs are a crucial component of the mRNA 5'-end capping quality control mechanism. They can possess RNA 5'-end pyrophosphohydrolase (PPH), decapping, and 5'-3' exonuclease (toward 5' monophosphate RNA) activities, which help to degrade mRNAs with incomplete 5'-end capping. A single active site in the enzyme supports these apparently distinct activities. However, each Rai1 protein studied so far has a unique set of activities, and the molecular basis for these differences are not known. Here, we have characterized the highly diverse activity profiles of Rai1 homologs from a collection of fungal organisms and identified a new activity for these enzymes, 5'-end triphosphonucleotide hydrolase (TPH) instead of PPH activity. Crystal structures of two of these enzymes bound to RNA oligonucleotides reveal differences in the RNA binding modes. Structure-based mutations of these enzymes, changing residues that contact the RNA but are poorly conserved, have substantial effects on their activity, providing a framework to begin to understand the molecular basis for the different activity profiles.
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Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes.,Wang VY, Jiao X, Kiledjian M, Tong L Nucleic Acids Res. 2015 Jun 22. pii: gkv620. PMID:26101253<ref>PMID:26101253</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Tong, L]]
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[[Category: Candida albicans SC5314]]
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[[Category: Wang, V Y]]
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[[Category: Large Structures]]
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[[Category: Decapping]]
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[[Category: Tong L]]
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[[Category: Hydrolase]]
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[[Category: Wang VY]]
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[[Category: Mrna 5'-processing]]
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[[Category: Rai1]]
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Current revision

Crystal structure of Candida albicans Rai1

PDB ID 5bth

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