5em2

Crystal structure of the Erb1-Ytm1 complex

spinqualitylabelsall models 5em2, resolution 2.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5em2 is a 4 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.67Å Ligands: EDO, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ERB1_CHATD Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.[HAMAP-Rule:MF_03027] Publication Abstract from PubMed The complicated process of eukaryotic ribosome biogenesis involves about 200 assembly factors that transiently associate with the nascent pre-ribosome in a spatiotemporally ordered way. During the early steps of 60S subunit formation, several proteins, collectively called A3 cluster factors, participate in the removal of the internal transcribed spacer 1 (ITS1) from 27SA3 pre-rRNA. Among these factors is the conserved hetero-trimeric Nop7-Erb1-Ytm1 complex (or human Pes1-Bop1-Wdr12), which is removed from the evolving pre-60S particle by the AAA ATPase Rea1 to allow progression in the pathway. Here, we clarify how Ytm1 and Erb1 interact, which has implications for the release mechanism of both factors from the pre-ribosome. Biochemical studies show that Ytm1 and Erb1 bind each other via their ss-propeller domains. The crystal structure of the Erb1-Ytm1 heterodimer determined at 2.67A resolution reveals an extended interaction surface between the propellers in a rarely observed binding mode. Structure-based mutations in the interface that impair the Erb1-Ytm1 interaction do not support growth, with specific defects in 60S subunit synthesis. Under these mutant conditions, it becomes clear that an intact Erb1-Ytm1 complex is required for 60S maturation and that loss of this stable interaction prevents ribosome production. Concerted removal of the Erb1-Ytm1 complex in ribosome biogenesis relies on an elaborate interface.,Thoms M, Ahmed YL, Maddi K, Hurt E, Sinning I Nucleic Acids Res. 2015 Dec 10. pii: gkv1365. PMID:26657628 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome biogenesis protein 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA