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Book Chapter: Structure of the MCM2-7 double hexamer and its implications for the mechanistic functions of the Mcm2-7 complex

TitleStructure of the MCM2-7 double hexamer and its implications for the mechanistic functions of the Mcm2-7 complex
Authors
KeywordsReplication licensing
MCM2-7
DNA replication
Cryo-EM structure
Issue Date2017
Citation
Advances in Experimental Medicine and Biology, 2017, v. 1042, p. 189-205 How to Cite?
Abstract© 2017, Springer Nature Singapore Pte Ltd. The eukaryotic minichromosome maintenance 2–7 complex is the core of the inactive MCM replication licensing complex and the catalytic core of the Cdc45-MCM-GINS replicative helicase. The years of effort to determine the structure of parts or the whole of the heterohexameric complex by X-ray crystallography and conventional cryo-EM produced limited success. Modern cryo-EM technology ushered in a new era of structural biology that allowed the determination of the structure of the inactive double hexamer at an unprecedented resolution of 3.8 Å. This review will focus on the fine details observed in the Mcm2-7 double hexameric complex and their implications for the function of the Mcm2-7 hexamer in its different roles during DNA replication.
Persistent Identifierhttp://hdl.handle.net/10722/255993
ISSN
2021 Impact Factor: 3.650
2023 SCImago Journal Rankings: 0.244
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhai, Yuanliang-
dc.contributor.authorTye, Bik Kwoon-
dc.date.accessioned2018-07-16T06:14:17Z-
dc.date.available2018-07-16T06:14:17Z-
dc.date.issued2017-
dc.identifier.citationAdvances in Experimental Medicine and Biology, 2017, v. 1042, p. 189-205-
dc.identifier.issn0065-2598-
dc.identifier.urihttp://hdl.handle.net/10722/255993-
dc.description.abstract© 2017, Springer Nature Singapore Pte Ltd. The eukaryotic minichromosome maintenance 2–7 complex is the core of the inactive MCM replication licensing complex and the catalytic core of the Cdc45-MCM-GINS replicative helicase. The years of effort to determine the structure of parts or the whole of the heterohexameric complex by X-ray crystallography and conventional cryo-EM produced limited success. Modern cryo-EM technology ushered in a new era of structural biology that allowed the determination of the structure of the inactive double hexamer at an unprecedented resolution of 3.8 Å. This review will focus on the fine details observed in the Mcm2-7 double hexameric complex and their implications for the function of the Mcm2-7 hexamer in its different roles during DNA replication.-
dc.languageeng-
dc.relation.ispartofAdvances in Experimental Medicine and Biology-
dc.subjectReplication licensing-
dc.subjectMCM2-7-
dc.subjectDNA replication-
dc.subjectCryo-EM structure-
dc.titleStructure of the MCM2-7 double hexamer and its implications for the mechanistic functions of the Mcm2-7 complex-
dc.typeBook_Chapter-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/978-981-10-6955-0_9-
dc.identifier.pmid29357059-
dc.identifier.scopuseid_2-s2.0-85041027282-
dc.identifier.hkuros288597-
dc.identifier.volume1042-
dc.identifier.spage189-
dc.identifier.epage205-
dc.identifier.eissn2214-8019-
dc.identifier.isiWOS:000438269000010-
dc.identifier.issnl0065-2598-

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