3RTY

Structure of an Enclosed Dimer Formed by The Drosophila Period Protein

3RTY の概要

• エントリーDOI: 10.2210/pdb3rty/pdb
• 分子名称: Period circadian protein, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• 機能のキーワード: pas domain, signalling, timeless, circadian clock protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Nucleus: P07663
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 309814.40

構造登録者

King, H.A.,Hoelz, A.,Crane, B.R.,Young, M.W. (登録日: 2011-05-04, 公開日: 2011-12-21, 最終更新日: 2024-12-25)

主引用文献

King, H.A.,Hoelz, A.,Crane, B.R.,Young, M.W.
Structure of an enclosed dimer formed by the Drosophila period protein.
J.Mol.Biol., 413:561-572, 2011

PubMed Abstract: Period (PER) is the major transcription inhibitor in metazoan circadian clocks and lies at the center of several feedback loops that regulate gene expression. Dimerization of Drosophila PER influences nuclear translocation, repressor activity, and behavioral rhythms. The structure of a central, 346-residue PER fragment reveals two associated PAS (Per-Arnt-Sim) domains followed by a protruding α-helical extension (αF). A closed, pseudo-symmetric dimer forms from a cross handshake interaction of the N-terminal PAS domain with αF of the opposing subunit. Strikingly, a shift of αF against the PAS β-sheet generates two alternative subunit interfaces in the dimer. Taken together with a previously reported PER structure in which αF extends, these data indicate that αF unlatches to switch association of PER with itself to its partner Timeless. The variable positions of the αF helix provide snapshots of a helix dissociation mechanism that has relevance to other PAS protein systems. Conservation of PER interaction residues among a family of PAS-AB-containing transcription factors suggests that contacts mediating closed PAS-AB dimers serve a general function.

PubMed: 21907720
DOI: 10.1016/j.jmb.2011.08.048

実験手法

X-RAY DIFFRACTION (2.85 Å)