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

Jiang, J., Zhang, Y., Krainer, A. R., Xu, R. M. (March 1999) Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein. Proceedings of the National Academy of Sciences of the United States of America, 96 (7). pp. 3572-7. ISSN 0027-8424 (Print)0027-8424

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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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals *Antigens, CD44 Caenorhabditis Carrier Proteins Computer Graphics Crystallography, X-Ray Humans Macromolecular Substances *Membrane Glycoproteins Mice Mitochondria/*metabolism Mitochondrial Proteins Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding *Protein Structure, Secondary Receptors, Complement/*chemistry/metabolism Recombinant Proteins/chemistry/metabolism Saccharomyces cerevisiae Sequence Alignment Sequence Homology, Amino Acid
Subjects: organs, tissues, organelles, cell types and functions > organelles, types and functions > mitochondria
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Krainer lab
CSHL labs > Xu lab
Depositing User: Matt Covey
Date: 30 March 1999
Date Deposited: 11 Mar 2014 20:14
Last Modified: 10 Sep 2019 19:44
PMCID: PMC22335
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29598

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