Studies of the fo membrane sector of atp synthase from escherichia coli

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Project objective

ATP synthase (F1F0- ATPase) is the central enzyme in energy conversion in mitochondria, chloroplasts and bacteria, driving the synthesis of ATP from ADP and inorganic phosphate. This multisubunit assembly consists of a globular domain, Fl (A group led by Dr.Walker has already determined the structure of F1-ATPase from bovine heart mitochondria), linked to an intrinsic membrane domain, F0. The long term aim is to establish the structure of the F0 membrane domain using the enzyme from E.coli. The simplest known F0 is found in E.coli. It consists of three subunits a","b" and "c" (a1b2c9-12). Subunits "a" and "e" are hydrophobic membrane proteins. Subunit "b" is a highly charged hydrophilic protein, which is thought to act as a central component in the interactions with F,. Over-expression of subunits "c" and "b" individually has been achieved, but neither F0 nor subunit "a" alone has yet been expressed successfully. The basis of the inestabitity will be first investigated, and once the problem has been overcome, the complex will be reconstituted. This will then permit the sites of interaction between the three subunits to be studied by mutation and cross-linking, and it will provide F0 for crystallization trials. "

Original text from CORDIS.

Participants

• MEDICAL RESEARCH COUNCIL · LONDONCoordinatorUnited Kingdom
• Not availableCity levelSpain

Links

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