1W5S

Structure of the Aeropyrum Pernix ORC2 protein (ADP form)

1W5S の概要

• エントリーDOI: 10.2210/pdb1w5s/pdb
• 関連するPDBエントリー: 1W5T
• 分子名称: ORIGIN RECOGNITION COMPLEX SUBUNIT 2 ORC2, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: replication, orc, cdc6, dna replication initiation, dna binding protein, aaa+ atpase
• 由来する生物種: AEROPYRUM PERNIX
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93829.45

構造登録者

Singleton, M.R.,Morales, R.,Grainge, I.,Cook, N.,Isupov, M.N.,Wigley, D.B. (登録日: 2004-08-09, 公開日: 2004-10-05, 最終更新日: 2024-05-08)

主引用文献

Singleton, M.R.,Morales, R.,Grainge, I.,Cook, N.,Isupov, M.N.,Wigley, D.B.
Conformational Changes Induced by Nucleotide Binding in Cdc6/Orc from Aeropyrum Pernix
J.Mol.Biol., 343:547-, 2004

PubMed Abstract: Archaea contain one or more proteins with homology to eukaryotic ORC/Cdc6 proteins. Sequence analysis suggests the existence of at least two subfamilies of these proteins, for which we propose the nomenclature ORC1 and ORC2. We have determined crystal structures of the ORC2 protein from the archaeon Aeropyrum pernix in complexes with ADP or a non-hydrolysable ATP analogue, ADPNP. Between two crystal forms, there are three crystallographically independent views of the ADP complex and two of the ADPNP complex. The protein molecules in the three complexes with ADP adopt very different conformations, while the two complexes with ADPNP are the same. These structures indicate that there is considerable conformational flexibility in ORC2 but that ATP binding stabilises a single conformation. We show that the ORC2 protein can bind DNA, and that this activity is associated with the C-terminal domain of the protein. We present a model for the interaction of the winged helix (WH) domain of ORC2 with DNA that differs from that proposed previously for Pyrobaculum aerophilum ORC/Cdc6.

PubMed: 15465044
DOI: 10.1016/J.JMB.2004.08.044

実験手法

X-RAY DIFFRACTION (2.4 Å)