Insights into the Architecture of the Replicative Helicase from the Structure of an Archaeal MCM Homolog

Brian Bae, Yi Hsing Chen, Alessandro Costa, Silvia Onesti, Joseph S. Brunzelle, Yuyen Lin, Isaac K.O. Cann, Satish K. Nair*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

The minichromosome maintenance (MCM) proteins, members of the AAA+ (ATPase associated with diverse cellular activities) superfamily, are believed to constitute the replicative helicase in eukaryotic and archaeal species. Here, we present the 1.9 Å resolution crystal structure of a monomeric MCM homolog from Methanopyrus kandleri, the first crystallographic structure of a full-length MCM. We also present an 18 Å cryo-electron microscopy reconstruction of the hexameric MCM from Methanothermobacter thermautotrophicus, and fit the atomic resolution crystal structure into the reconstruction in order to generate an atomic model for the oligomeric assembly. These structural data reveal a distinct active site topology consisting of a unique arrangement of critical determinants. The structures also provide a molecular framework for understanding the functional contributions of trans-acting elements that facilitate intersubunit crosstalk in response to DNA binding and ATP hydrolysis.

Original languageEnglish (US)
Pages (from-to)211-222
Number of pages12
JournalStructure
Volume17
Issue number2
DOIs
StatePublished - Feb 13 2009

Keywords

  • DNA

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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