3F8T

Crystal structure analysis of a full-length MCM homolog from Methanopyrus kandleri

Summary for 3F8T

• Entry DOI: 10.2210/pdb3f8t/pdb
• Descriptor: Predicted ATPase involved in replication control, Cdc46/Mcm family (2 entities in total)
• Functional Keywords: mcm, helicase, mcm homolog, dna replication, atp-binding, dna-binding, nucleotide-binding, hydrolase
• Biological source: Methanopyrus kandleri AV19
• Total number of polymer chains: 1
• Total formula weight: 56633.64

Authors

Bae, B.,Nair, S.K. (deposition date: 2008-11-13, release date: 2009-03-03, Last modification date: 2023-12-27)

Primary citation

Bae, B.,Chen, Y.H.,Costa, A.,Onesti, S.,Brunzelle, J.S.,Lin, Y.,Cann, I.K.,Nair, S.K.
Insights into the Architecture of the Replicative Helicase from the Structure of an Archaeal MCM Homolog.
Structure, 17:211-222, 2009

PubMed 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 A 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 A 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.

PubMed: 19217392
DOI: 10.1016/j.str.2008.11.010

Experimental method

X-RAY DIFFRACTION (1.9 Å)