Poly(A) RNA polymerase

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spinqualitylabelsall models Cid1 complex with UTP (stick model) (PDB code 4e80) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Poly(A) RNA polymerase protein Cid1 (Caffeine-Induced Death protein 1) is involved in cell cycle arrest where it inhibits unscheduled mitosis[1]. Cid1 is found in fission yeast. Cid1 exists in 3 forms: apo I consists of 4 subunits; apo II consists of 2 subunits; UTP-bound form consists of 4 subunits. The UTP-bound form has in its N-terminal domain a catalytic triad of Asp residues which bind the UTP. Structural highlights The UTP binding site of Cid1 is between the N-terminal and C-terminal. The active site contains the catalytic triad aspirates and the His residue whose two conformations select between binding of UTP and ATP [2].

3D Structures of poly(A) RNA polymerase protein Cid1

Updated on 05-July-2016

4e7x, 4e8f – Cid1
4ud4, 4ud5 – Cid1 (mutant)
4e80 – Cid1 + UTP
4fh3 – Cid1 residues 33-377
4ep7, 4fh5, 4fhp – Cid1 residues 30-377 + UTP
4fhv – Cid1 residues 30-377 + CTP
4fhw – Cid1 residues 30-377 + GTP
4fhy – Cid1 residues 30-377 + ATP
4fhx – Cid1 residues 30-377 (mutant) + ATP
4nkt – Cid1 residues 30-377 + UMPNPP
4nku – Cid1 residues 40-377 (mutant) + dinucleotide

References

1. ↑ Stevenson AL, Norbury CJ. The Cid1 family of non-canonical poly(A) polymerases. Yeast. 2006 Oct 15;23(13):991-1000. PMID:17072891 doi:http://dx.doi.org/10.1002/yea.1408
2. ↑ Yates LA, Fleurdepine S, Rissland OS, De Colibus L, Harlos K, Norbury CJ, Gilbert RJ. Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase. Nat Struct Mol Biol. 2012 Jul 1. doi: 10.1038/nsmb.2329. PMID:22751018 doi:10.1038/nsmb.2329