In this section
@article{Yuan:2017:10.1038/nsmb.3372,
author = {Yuan, Z and Riera, A and Bai, L and Sun, J and Nandi, S and Spanos, C and Chen, ZA and Barbon, M and Rappsilber, J and Stillman, B and Speck, C and Li, H},
doi = {10.1038/nsmb.3372},
journal = {Nature Structural & Molecular Biology},
pages = {316--324},
title = {Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1},
url = {http://dx.doi.org/10.1038/nsmb.3372},
volume = {24},
year = {2017}
}
TY - JOUR
AB - To start DNA replication, the Origin Recognition Complex (ORC) and Cdc6 load a Mcm2-7 double hexamer onto DNA. Without ATP hydrolysis, ORC-Cdc6 recruits one Cdt1-bound Mcm2-7 hexamer, forming an ORC-Cdc6-Cdt1-Mcm2-7 (OCCM) helicase loading intermediate. Here we report a 3.9Å structure of the OCCM on DNA. Flexible Mcm2-7 winged-helix domains (WHD) engage ORC-Cdc6. A three-domain Cdt1 configuration embraces Mcm2, Mcm4, and Mcm6, nearly half of the hexamer. The Cdt1 C-terminal domain extends to the Mcm6 WHD, which binds Orc4 WHD. DNA passes through the ORC-Cdc6 and Mcm2-7 rings. Origin DNA interaction is mediated by an a-helix in Orc4 and positively charged loops in Orc2 and Cdc6. The Mcm2-7 C-tier AAA+ ring is topologically closed by a Mcm5 loop that embraces Mcm2, but the N-tier ring Mcm2-Mcm5 interface remains open. This structure suggests loading mechanics of the first Cdt1-bound Mcm2-7 hexamer by ORC-Cdc6.
AU - Yuan,Z
AU - Riera,A
AU - Bai,L
AU - Sun,J
AU - Nandi,S
AU - Spanos,C
AU - Chen,ZA
AU - Barbon,M
AU - Rappsilber,J
AU - Stillman,B
AU - Speck,C
AU - Li,H
DO - 10.1038/nsmb.3372
EP - 324
PY - 2017///
SN - 1545-9993
SP - 316
TI - Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1
T2 - Nature Structural & Molecular Biology
UR - http://dx.doi.org/10.1038/nsmb.3372
UR - https://www.nature.com/articles/nsmb.3372
UR - http://hdl.handle.net/10044/1/43837
VL - 24
ER -
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