CULLIN_2 domain-containing protein / RING-type domain-containing protein / Leucine rich repeat protein 1 L homeolog isoform X1 / Elongin B L homeolog / Elongin-C Similarity search - Component
Biological species
Xenopus laevis (African clawed frog)
Method
single particle reconstruction / cryo EM / Resolution: 3.1 Å
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM141109
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM80676
United States
Citation
Journal: Nucleic Acids Res / Year: 2021 Title: Structure of CRL2Lrr1, the E3 ubiquitin ligase that promotes DNA replication termination in vertebrates. Authors: Haixia Zhou / Manal S Zaher / Johannes C Walter / Alan Brown / Abstract: When vertebrate replisomes from neighboring origins converge, the Mcm7 subunit of the replicative helicase, CMG, is ubiquitylated by the E3 ubiquitin ligase, CRL2Lrr1. Polyubiquitylated CMG is then ...When vertebrate replisomes from neighboring origins converge, the Mcm7 subunit of the replicative helicase, CMG, is ubiquitylated by the E3 ubiquitin ligase, CRL2Lrr1. Polyubiquitylated CMG is then disassembled by the p97 ATPase, leading to replication termination. To avoid premature replisome disassembly, CRL2Lrr1 is only recruited to CMGs after they converge, but the underlying mechanism is unclear. Here, we use cryogenic electron microscopy to determine structures of recombinant Xenopus laevis CRL2Lrr1 with and without neddylation. The structures reveal that CRL2Lrr1 adopts an unusually open architecture, in which the putative substrate-recognition subunit, Lrr1, is located far from the catalytic module that catalyzes ubiquitin transfer. We further demonstrate that a predicted, flexible pleckstrin homology domain at the N-terminus of Lrr1 is essential to target CRL2Lrr1 to terminated CMGs. We propose a hypothetical model that explains how CRL2Lrr1's catalytic module is positioned next to the ubiquitylation site on Mcm7, and why CRL2Lrr1 binds CMG only after replisomes converge.
History
Deposition
Oct 9, 2021
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Header (metadata) release
Dec 8, 2021
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Map release
Dec 8, 2021
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Update
Jun 5, 2024
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Current status
Jun 5, 2024
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Cryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 281.2 K / Instrument: FEI VITROBOT MARK IV / Details: Blot 6 seconds with the force 12.
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 54.5 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron optics
Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
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