5YVF

Crystal structure of BFA1

Summary for 5YVF

• Entry DOI: 10.2210/pdb5yvf/pdb
• Descriptor: BFA1 (2 entities in total)
• Functional Keywords: atp synthase, assembly, fba1, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 4
• Total formula weight: 167807.97

Authors

Pu, H.,Zhang, L.,Duan, Z.K.,Peng, L.W.,Liu, L. (deposition date: 2017-11-25, release date: 2018-08-08, Last modification date: 2024-03-27)

Primary citation

Zhang, L.,Pu, H.,Duan, Z.,Li, Y.,Liu, B.,Zhang, Q.,Li, W.,Rochaix, J.D.,Liu, L.,Peng, L.
Nucleus-Encoded Protein BFA1 Promotes Efficient Assembly of the Chloroplast ATP Synthase Coupling Factor 1.
Plant Cell, 30:1770-1788, 2018

PubMed Abstract: F-type ATP synthases produce nearly all of the ATP found in cells. The catalytic module F commonly comprises an αβ hexamer surrounding a γ/ε stalk. However, it is unclear how these subunits assemble to form a catalytic motor. In this work, we identified and characterized a chloroplast protein that interacts with the CFβ, γ, and ε subunits of the chloroplast ATP synthase and is required for assembly of its F module. We named this protein BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE1 (BFA1) and determined its crystal structure at 2.8-Å resolution. BFA1 is comprised primarily of two interacting β-barrels that are oriented nearly perpendicularly to each other. The contact region between BFA1 and the CFβ and γ subunits was further mapped by yeast two-hybrid assays. An in silico molecular docking analysis was performed and revealed close fitting contact sites without steric conflicts between BFA1 and CFβ/γ. We propose that BFA1 acts mainly as a scaffold protein promoting the association of a CFα/β heterodimer with CFγ. The subsequent assembly of other CFα/β heterodimers may shift the position of the CFγ subunit to complete assembly of the CF module. This CF assembly process is likely to be valid for other F-type ATP synthases, as their structures are highly conserved.

PubMed: 30012777
DOI: 10.1105/tpc.18.00075

Experimental method

X-RAY DIFFRACTION (2.804 Å)