2QI2

Crystal structure of the Thermoplasma acidophilum Pelota protein

Summary for 2QI2

• Entry DOI: 10.2210/pdb2qi2/pdb
• Descriptor: Cell division protein pelota related protein (2 entities in total)
• Functional Keywords: pelota, dom34, cell cycle
• Biological source: Thermoplasma acidophilum
• Cellular location: Cytoplasm (Potential): Q9HJ74
• Total number of polymer chains: 1
• Total formula weight: 39526.28

Authors

Lee, H.H.,Kim, Y.S.,Kim, K.H.,Heo, I.H.,Kim, S.K.,Kim, O.,Suh, S.W. (deposition date: 2007-07-03, release date: 2007-10-09, Last modification date: 2024-03-13)

Primary citation

Lee, H.H.,Kim, Y.S.,Kim, K.H.,Heo, I.,Kim, S.K.,Kim, O.,Kim, H.K.,Yoon, J.Y.,Kim, H.S.,Kim, D.J.,Lee, S.J.,Yoon, H.J.,Kim, S.J.,Lee, B.G.,Song, H.K.,Kim, V.N.,Park, C.M.,Suh, S.W.
Structural and functional insights into dom34, a key component of no-go mRNA decay
Mol.Cell, 27:938-950, 2007

PubMed Abstract: The yeast protein Dom34 is a key component of no-go decay, by which mRNAs with translational stalls are endonucleolytically cleaved and subsequently degraded. However, the identity of the endoribonuclease is unknown. Homologs of Dom34, called Pelota, are broadly conserved in eukaryotes and archaea. To gain insights into the structure and function of Dom34/Pelota, we have determined the structure of Pelota from Thermoplasma acidophilum (Ta Pelota) and investigated the ribonuclease activity of Dom34/Pelota. The structure of Ta Pelota is tripartite, and its domain 1 has the RNA-binding Sm fold. We have discovered that Ta Pelota has a ribonuclease activity and that its domain 1 is sufficient for the catalytic activity. We also demonstrate that domain 1 of Dom34 has an endoribonuclease activity against defined RNA substrates containing a stem loop, which supports a direct catalytic role of yeast Dom34 in no-go mRNA decay.

PubMed: 17889667
DOI: 10.1016/j.molcel.2007.07.019

Experimental method

X-RAY DIFFRACTION (2.9 Å)