The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings.

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TitleThe Methanobacterium thermoautotrophicum MCM protein can form heptameric rings.
Publication TypeJournal Article
Year of Publication2002
AuthorsYu, X, VanLoock, MS, Poplawski, A, Kelman, Z, Xiang, T, Tye, BK, Egelman, EH
JournalEMBO Rep
Volume3
Issue8
Pagination792-7
Date Published2002 Aug
ISSN1469-221X
KeywordsAmino Acid Motifs, Archaeal Proteins, Crystallography, X-Ray, DNA, DNA Helicases, Escherichia coli, Methanobacterium, Microscopy, Electron, Models, Molecular, Protein Structure, Tertiary
Abstract

Mini-chromosome maintenance (MCM) proteins form a conserved family found in all eukaryotes and are essential for DNA replication. They exist as heteromultimeric complexes containing as many as six different proteins. These complexes are believed to be the replicative helicases, functioning as hexameric rings at replication forks. In most archaea a single MCM protein exists. The protein from Methanobacterium thermoautotrophicum (mtMCM) has been reported to assemble into a large complex consistent with a dodecamer. We show that mtMCM can assemble into a heptameric ring. This ring contains a C-terminal helicase domain that can be fit with crystal structures of ring helicases and an N-terminal domain of unknown function. While the structure of the ring is very similar to that of hexameric replicative helicases such as bacteriophage T7 gp4, our results show that such ring structures may not be constrained to have only six subunits.

DOI10.1093/embo-reports/kvf160
Alternate JournalEMBO Rep.
PubMed ID12151340
PubMed Central IDPMC1084214
Grant ListGM34190 / GM / NIGMS NIH HHS / United States
GM35269 / GM / NIGMS NIH HHS / United States