1WA9

Crystal Structure of the PAS repeat region of the Drosophila clock protein PERIOD

Summary for 1WA9

• Entry DOI: 10.2210/pdb1wa9/pdb
• Descriptor: PERIOD CIRCADIAN PROTEIN (2 entities in total)
• Functional Keywords: period, pas domain, circadian rhythm, clock protein, phosphorylation, polymorphism
• Biological source: DROSOPHILA MELANOGASTER (FRUIT FLY)
• Cellular location: Nucleus: P07663
• Total number of polymer chains: 2
• Total formula weight: 82914.94

Authors

Yildiz, O.,Doi, M.,Yujnovsky, I.,Cardone, L.,Berndt, A.,Hennig, S.,Schulze, S.,Urbanke, C.,Sassone-Corsi, P.,Wolf, E. (deposition date: 2004-10-25, release date: 2005-01-12, Last modification date: 2024-05-08)

Primary citation

Yildiz, O.,Doi, M.,Yujnovsky, I.,Cardone, L.,Berndt, A.,Hennig, S.,Schulze, S.,Urbanke, C.,Sassone-Corsi, P.,Wolf, E.
Crystal Structure and Interactions of the Pas Repeat Region of the Drosophila Clock Protein Period
Mol.Cell, 17:69-, 2005

PubMed Abstract: PERIOD proteins are central components of the Drosophila and mammalian circadian clock. Their function is controlled by daily changes in synthesis, cellular localization, phosphorylation, degradation, as well as specific interactions with other clock components. Here we present the crystal structure of a Drosophila PERIOD (dPER) fragment comprising two tandemly organized PAS (PER-ARNT-SIM) domains (PAS-A and PAS-B) and two additional C-terminal alpha helices (alphaE and alphaF). Our analysis reveals a noncrystallographic dPER dimer mediated by intermolecular interactions of PAS-A with PAS-B and helix alphaF. We show that alphaF is essential for dPER homodimerization and that the PAS-A-alphaF interaction plays a crucial role in dPER clock function, as it is affected by the 29 hr long-period perL mutation.

PubMed: 15629718
DOI: 10.1016/J.MOLCEL.2004.11.022

Experimental method

X-RAY DIFFRACTION (3.15 Å)