3SDJ

Structure of RNase-inactive point mutant of oligomeric kinase/RNase Ire1

Summary for 3SDJ

• Entry DOI: 10.2210/pdb3sdj/pdb
• Related: 3SDM 3fbv
• Descriptor: Serine/threonine-protein kinase/endoribonuclease IRE1, N~2~-1H-benzimidazol-5-yl-N~4~-(3-cyclopropyl-1H-pyrazol-5-yl)pyrimidine-2,4-diamine (2 entities in total)
• Functional Keywords: kinase, rnase, ribonuclease, hac1, xbp1, splicing, rna, upr, unfolded protein response, oligomer, transferase, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 14
• Total formula weight: 730683.95

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: 2024-11-06)

Primary citation

Korennykh, A.V.,Korostelev, A.A.,Egea, P.F.,Finer-Moore, J.,Stroud, R.M.,Zhang, C.,Shokat, K.M.,Walter, P.
Structural and functional basis for RNA cleavage by Ire1.
Bmc Biol., 9:47-47, 2011

PubMed Abstract: The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1. The endoribonuclease (RNase) domain of Ire1 initiates a non-conventional mRNA splicing reaction, leading to the production of a transcription factor that controls UPR target genes. The mRNA splicing reaction is an obligatory step of Ire1 signaling, yet its mechanism has remained poorly understood due to the absence of substrate-bound crystal structures of Ire1, the lack of structural similarity between Ire1 and other RNases, and a scarcity of quantitative enzymological data. Here, we experimentally define the active site of Ire1 RNase and quantitatively evaluate the contribution of the key active site residues to catalysis.

PubMed: 21729333
DOI: 10.1186/1741-7007-9-47

Experimental method

X-RAY DIFFRACTION (3.65 Å)