3F9V

Crystal Structure Of A Near Full-Length Archaeal MCM: Functional Insights For An AAA+ Hexameric Helicase

3F9V の概要

• エントリーDOI: 10.2210/pdb3f9v/pdb
• 分子名称: Minichromosome maintenance protein MCM (1 entity in total)
• 機能のキーワード: replicative helicase, dna replication, mcm complex, aaa+ protein, atp-binding, dna-binding, helicase, hydrolase, nucleotide-binding
• 由来する生物種: Sulfolobus solfataricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67318.62

構造登録者

Chen, X.J.,Brewster, A.S.,Wang, G.G.,Yu, X.,Greenleaf, W.,Tjajadi, M.,Klein, M. (登録日: 2008-11-14, 公開日: 2008-12-30, 最終更新日: 2023-12-27)

主引用文献

Brewster, A.S.,Wang, G.,Yu, X.,Greenleaf, W.B.,Carazo, J.M.,Tjajadia, M.,Klein, M.G.,Chen, X.S.
Crystal structure of a near-full-length archaeal MCM: Functional insights for an AAA+ hexameric helicase.
Proc.Natl.Acad.Sci.USA, 105:20191-20196, 2008

PubMed Abstract: The minichromosome maintenance protein (MCM) complex is an essential replicative helicase for DNA replication in Archaea and Eukaryotes. Whereas the eukaryotic complex consists of 6 homologous proteins (MCM2-7), the archaeon Sulfolobus solfataricus has only 1 MCM protein (ssoMCM), 6 subunits of which form a homohexamer. Here, we report a 4.35-A crystal structure of the near-full-length ssoMCM. The structure shows an elongated fold, with 5 subdomains that are organized into 2 large N- and C-terminal domains. A near-full-length ssoMCM hexamer generated based on the 6-fold symmetry of the N-terminal Methanothermobacter thermautotrophicus (mtMCM) hexamer shows intersubunit distances suitable for bonding contacts, including the interface around the ATP pocket. Four unusual beta-hairpins of each subunit are located inside the central channel or around the side channels in the hexamer. Additionally, the hexamer fits well into the double-hexamer EM map of mtMCM. Our mutational analysis of residues at the intersubunit interfaces and around the side channels demonstrates their critical roles for hexamerization and helicase function. These structural and biochemical results provide a basis for future study of the helicase mechanisms of the archaeal and eukaryotic MCM complexes in DNA replication.

PubMed: 19073923
DOI: 10.1073/pnas.0808037105

実験手法

X-RAY DIFFRACTION (4.35 Å)