The Methanothermobacter thermautotrophicus MCM helicase is active as a hexameric ring.
The minichromosome maintenance (MCM) complex is thought to function as the replicative helicase in archaea and eukarya. The structure of the single MCM protein homologue from the archaeon Methanothermobacter thermautotrophicus is not yet clear, and hexameric, heptameric, octameric, and dodecameric structures, open rings, and filamentous structures have been reported. Using a combination of biochemical and structural analysis, it is shown here that the M. thermautotrophicus MCM helicase is active as a hexamer.
Shin
Jae-Ho
JH
Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University, 1370 Sankyuk-Dong, Daegu 702-701, Republic of Korea and the University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology, Rockville, Maryland 20850.
Heo
Gun-Young
GY
Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University, 1370 Sankyuk-Dong, Daegu 702-701, Republic of Korea and the University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology, Rockville, Maryland 20850.
Kelman
Zvi
Z
Division of Applied Biology and Chemistry, College of Agriculture and Life Sciences, Kyungpook National University, 1370 Sankyuk-Dong, Daegu 702-701, Republic of Korea and the University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology, Rockville, Maryland 20850. Electronic address: kelman@umbi.umd.edu.
D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D019847:Chromosomes, Archaeal / Q000378:metabolism; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism; D017013:Methanobacteriaceae / Q000201:enzymology*; D020836:Protein Structure, Quaternary / Q000502:physiology; D013329:Structure-Activity Relationship
D019843:Archaeal Proteins; D004265:DNA Helicases; C403162:MCM protein, Methanobacterium thermoautotrophicum