The Methanobacterium thermoautotrophicum MCM protein can form heptameric rings

• Published in: EMBO reports Vol. 3; no. 8; pp. 792 - 797
• Main Authors: Yu, Xiong, VanLoock, Margaret S, Poplawski, Andrzej, Kelman, Zvi, Xiang, Tao, Tye, Bik K, Egelman, Edward H
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01-08-2002; Blackwell Publishing Ltd; Oxford University Press
• Subjects: Amino Acid Motifs; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Crystallography, X-Ray; DNA - biosynthesis; DNA Helicases - chemistry; DNA Helicases - metabolism; Escherichia coli - metabolism; Methanobacterium - metabolism; Methanobacterium - ultrastructure; Microscopy, Electron; Models, Molecular; Protein Structure, Tertiary; Scientific Reports
• ISSN: 1469-221X; 1469-3178
• DOI: 10.1093/embo-reports/kvf160

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.