Ontology highlight
ABSTRACT:
SUBMITTER: Jiang J
PROVIDER: S-EPMC22335 | biostudies-literature | 1999 Mar
REPOSITORIES: biostudies-literature
Jiang J J Zhang Y Y Krainer A R AR Xu R M RM
Proceedings of the National Academy of Sciences of the United States of America 19990301 7
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-helic ...[more]