4ud5: Difference between revisions
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<StructureSection load='4ud5' size='340' side='right'caption='[[4ud5]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='4ud5' size='340' side='right'caption='[[4ud5]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ud5]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ud5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UD5 FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ud5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud5 OCA], [https://pdbe.org/4ud5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ud5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ud5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud5 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CID1_SCHPO CID1_SCHPO] Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]] | *[[Poly(A) RNA polymerase|Poly(A) RNA polymerase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Durrant | [[Category: Schizosaccharomyces pombe]] | ||
[[Category: Fleurdepine | [[Category: Durrant BP]] | ||
[[Category: Gilbert | [[Category: Fleurdepine S]] | ||
[[Category: Harlos | [[Category: Gilbert RJC]] | ||
[[Category: Norbury | [[Category: Harlos K]] | ||
[[Category: Yates | [[Category: Norbury CJ]] | ||
[[Category: Yates LA]] | |||
Revision as of 11:17, 22 March 2023
Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase ActivityStructural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase Activity
Structural highlights
FunctionCID1_SCHPO Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis. Publication Abstract from PubMedTerminal uridylyl transferases (TUTs) are responsible for the post-transcriptional addition of uridyl residues to RNA 3' ends, leading in some cases to altered stability. The Schizosaccharomyces pombe TUT Cid1 is a model enzyme that has been characterized structurally at moderate resolution and provides insights into the larger and more complex mammalian TUTs, ZCCHC6 and ZCCHC11. Here, we report a higher resolution (1.74 A) crystal structure of Cid1 that provides detailed evidence for uracil selection via the dynamic flipping of a single histidine residue. We also describe a novel closed conformation of the enzyme that may represent an intermediate stage in a proposed product ejection mechanism. The structural insights gained, combined with normal mode analysis and biochemical studies, demonstrate that the plasticity of Cid1, particularly about a hinge region (N164-N165), is essential for catalytic activity, and provide an explanation for its distributive uridylyl transferase activity. We propose a model clarifying observed differences between the in vitro apparently processive activity and in vivo distributive monouridylylation activity of Cid1. We suggest that modulating the flexibility of such enzymes-for example by the binding of protein co-factors-may allow them alternatively to add single or multiple uridyl residues to the 3' termini of RNA molecules. Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.,Yates LA, Durrant BP, Fleurdepine S, Harlos K, Norbury CJ, Gilbert RJ Nucleic Acids Res. 2015 Mar 11;43(5):2968-79. doi: 10.1093/nar/gkv122. Epub 2015 , Feb 20. PMID:25712096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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