3SDM

Structure of oligomeric kinase/RNase Ire1 in complex with an oligonucleotide

Summary for 3SDM

• Entry DOI: 10.2210/pdb3sdm/pdb
• Related: 3fbv 3sdj
• Descriptor: Serine/threonine-protein kinase/endoribonuclease IRE1 (1 entity in total)
• Functional Keywords: kinase, rnase, ribonuclease, hac1, xbp1, splicing, rna, upr, unfolded protein response, oligomer, complex, oligonucleotide, transferase, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 7
• Total formula weight: 363183.74

Authors

Korennykh, A.,Korostelev, A.,Egea, P.,Finer-Moore, J.,Zhang, C.,Stroud, R.,Shokat, K.,Walter, P. (deposition date: 2011-06-09, release date: 2011-07-13, Last modification date: 2024-11-20)

Primary citation

Korennykh, A.V.,Egea, P.F.,Korostelev, A.A.,Finer-Moore, J.,Stroud, R.M.,Zhang, C.,Shokat, K.M.,Walter, P.
Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1.
Bmc Biol., 9:48-48, 2011

PubMed Abstract: Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell. Ire1 signals, in a transcriptional program, the unfolded protein response (UPR) via the coordinated action of its protein kinase and RNase domains. In this study, we investigated how the binding of cofactors to the kinase domain of Ire1 modulates its RNase activity.

PubMed: 21729334
DOI: 10.1186/1741-7007-9-48

Experimental method

X-RAY DIFFRACTION (6.6 Å)