4ud4: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ud4]] 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=4UD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UD4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ud4]] 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=4UD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UD4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4ud4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud4 OCA], [https://pdbe.org/4ud4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ud4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ud4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud4 ProSAT]</span></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=4ud4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud4 OCA], [https://pdbe.org/4ud4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ud4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ud4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud4 ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 15:28, 20 December 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

4ud4 is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.74Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CID1_SCHPO Involved in cell cycle arrest where in association with crb2/rhp9 and chk1 it inhibits unscheduled mitosis.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Yates LA, Durrant BP, Fleurdepine S, Harlos K, Norbury CJ, Gilbert RJ. Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity. Nucleic Acids Res. 2015 Mar 11;43(5):2968-79. doi: 10.1093/nar/gkv122. Epub 2015 , Feb 20. PMID:25712096 doi:http://dx.doi.org/10.1093/nar/gkv122

4ud4, resolution 1.74Å

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OCA