1ltl
From Proteopedia
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THE DODECAMER STRUCTURE OF MCM FROM ARCHAEAL M. THERMOAUTOTROPHICUM
Overview
Eukaryotic chromosomal DNA is licensed for replication precisely once in, each cell cycle. The mini-chromosome maintenance (MCM) complex plays a, role in this replication licensing. We have determined the structure of a, fragment of MCM from Methanobacterium thermoautotrophicum (mtMCM), a model, system for eukaryotic MCM. The structure reveals a novel dodecameric, architecture with a remarkably long central channel. The channel surface, has an unusually high positive charge and binds DNA. We also show that the, structure of the N-terminal fragment is conserved for all MCMs proteins, despite highly divergent sequences, suggesting a common architecture for a, similar task: gripping/remodeling DNA and regulating MCM activity. An, mtMCM mutant protein equivalent to a yeast MCM5 (CDC46) protein with the, bob1 mutation at its N terminus has only subtle structural changes, suggesting a Cdc7-bypass mechanism by Bob1 in yeast. Yeast bypass, experiments using MCM5 mutant proteins support the hypothesis for the, bypass mechanism.
About this Structure
1LTL is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
The structure and function of MCM from archaeal M. Thermoautotrophicum., Fletcher RJ, Bishop BE, Leon RP, Sclafani RA, Ogata CM, Chen XS, Nat Struct Biol. 2003 Mar;10(3):160-7. PMID:12548282
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