4ud5: Difference between revisions
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''' | ==Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase Activity== | ||
<StructureSection load='4ud5' size='340' side='right' caption='[[4ud5]], [[Resolution|resolution]] 2.52Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ud5]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UD5 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ud4|4ud4]]</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=4ud5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ud5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ud5 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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;"> | |||
== Publication Abstract from PubMed == | |||
Terminal 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<ref>PMID:25712096</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: Durrant, B P]] | |||
[[Category: Fleurdepine, S]] | [[Category: Fleurdepine, S]] | ||
[[Category: | [[Category: Gilbert, R J.C]] | ||
[[Category: Harlos, K]] | [[Category: Harlos, K]] | ||
[[Category: Norbury, C J]] | |||
[[Category: Yates, L A]] | |||
[[Category: Caffeine]] | |||
[[Category: Transferase]] | |||
[[Category: Uridylyltransferase enzyme]] | |||
Revision as of 15:02, 18 March 2015
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
Function[CID1_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. References
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