3Q8T

Crystal structure of the coiled coil domain of Beclin 1, an essential autophagy protein

Summary for 3Q8T

• Entry DOI: 10.2210/pdb3q8t/pdb
• Descriptor: Beclin-1 (2 entities in total)
• Functional Keywords: autophagy, atg14l uvrag, apoptosis
• Biological source: Rattus norvegicus (rat)
• Cellular location: Cytoplasm: Q91XJ1
• Total number of polymer chains: 2
• Total formula weight: 23055.54

Authors

Li, X.,Zhao, Y. (deposition date: 2011-01-07, release date: 2012-01-18, Last modification date: 2024-03-20)

Primary citation

Li, X.,He, L.,Che, K.H.,Funderburk, S.F.,Pan, L.,Pan, N.,Zhang, M.,Yue, Z.,Zhao, Y.
Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG
Nat Commun, 3:662-662, 2012

PubMed Abstract: Beclin 1 is a core component of the Class III Phosphatidylinositol 3-Kinase VPS34 complex. The coiled coil domain of Beclin 1 serves as an interaction platform for assembly of distinct Atg14L- and UVRAG-containing complexes to modulate VPS34 activity. Here we report the crystal structure of the coiled coil domain that forms an antiparallel dimer and is rendered metastable by a series of 'imperfect' a-d' pairings at its coiled coil interface. Atg14L and UVRAG promote the transition of metastable homodimeric Beclin 1 to heterodimeric Beclin1-Atg14L/UVRAG assembly. Beclin 1 mutants with their 'imperfect' a-d' pairings modified to enhance self-interaction, show distinctively altered interactions with Atg14L or UVRAG. These results suggest that specific utilization of the dimer interface and modulation of the homodimer-heterodimer transition by Beclin 1-interacting partners may underlie the molecular mechanism that controls the formation of various Beclin1-VPS34 subcomplexes to exert their effect on an array of VPS34-related activities, including autophagy.

PubMed: 22314358
DOI: 10.1038/ncomms1648

Experimental method

X-RAY DIFFRACTION (1.9 Å)