Work

Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein

Year: 1999

Type: article

Abstract: Human p32 (also known as SF2-associated p32, p32/TAP, and gC1qR) is a conserved eukaryotic protein that localizes predominantly in the mitochondrial matrix. It is thought to be involved in mitochondrial oxidative phosphorylation and in nucleus-mitochondrion interactions. We report the crystal structure of p32 determined at 2.25 A resolution. The structure reveals that p32 adopts a novel fold with seven consecutive antiparallel beta-strands flanked by one N-terminal and two C-terminal alpha-helices. Three monomers form a doughnut-shaped quaternary structure with an unusually asymmetric charge distribution on the surface. The implications of the structure on previously proposed functions of p32 are discussed and new specific functional properties are suggested.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.96.7.3572

Authors: Jianzhong Jiang, Ying Zhang, Adrian R. Krainer, Rui-Ming Xu

Institutions: Cold Spring Harbor Laboratory, Stony Brook University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green