5bth: Difference between revisions
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''' | ==Crystal structure of Candida albicans Rai1== | ||
<StructureSection load='5bth' size='340' side='right' caption='[[5bth]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</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> | |||
<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> | |||
</table> | |||
== Function == | |||
[[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Tong, L]] | [[Category: Tong, L]] | ||
[[Category: Wang, V | [[Category: Wang, V Y]] | ||
[[Category: Decapping]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mrna 5'-processing]] | |||
[[Category: Rai1]] | |||
Revision as of 14:48, 8 July 2015
Crystal structure of Candida albicans Rai1
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