2ey4
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Crystal Structure of a Cbf5-Nop10-Gar1 Complex
OverviewOverview
H/ACA RNA-protein complexes, comprised of four proteins and an H/ACA guide, RNA, modify ribosomal and small nuclear RNAs. The H/ACA proteins are also, essential components of telomerase in mammals. Cbf5 is the H/ACA protein, that catalyzes isomerization of uridine to pseudouridine in target RNAs., Mutations in human Cbf5 (dyskerin) lead to dyskeratosis congenita. Here, we describe the 2.1 A crystal structure of a specific complex of three, archaeal H/ACA proteins, Cbf5, Nop10, and Gar1. Cbf5 displays structural, properties that are unique among known pseudouridine synthases and are, consistent with its distinct function in RNA-guided pseudouridylation. We, also describe the previously unknown structures of both Nop10 and Gar1 and, the structural basis for their essential roles in pseudouridylation. By, using information from related structures, we have modeled the entire, ribonucleoprotein complex including both guide and substrate RNAs. We have, also identified a dyskeratosis congenita mutation cluster site within a, modeled dyskerin structure.
About this StructureAbout this Structure
2EY4 is a Protein complex structure of sequences from Pyrococcus furiosus and Pyrococcus furiosus dsm 3638 with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita., Rashid R, Liang B, Baker DL, Youssef OA, He Y, Phipps K, Terns RM, Terns MP, Li H, Mol Cell. 2006 Jan 20;21(2):249-60. PMID:16427014
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