3F8T

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

3F8T の概要

• エントリーDOI: 10.2210/pdb3f8t/pdb
• 分子名称: Predicted ATPase involved in replication control, Cdc46/Mcm family (2 entities in total)
• 機能のキーワード: mcm, helicase, mcm homolog, dna replication, atp-binding, dna-binding, nucleotide-binding, hydrolase
• 由来する生物種: Methanopyrus kandleri AV19
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56633.64

構造登録者

Bae, B.,Nair, S.K. (登録日: 2008-11-13, 公開日: 2009-03-03, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)