1p32

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p32 OCA], [http://www.ebi.ac.uk/pdbsum/1p32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p32 RCSB]</span>
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[[Category: mitochondrial matrix protein]]
[[Category: mitochondrial matrix protein]]
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Revision as of 19:54, 30 March 2008


PDB ID 1p32

Drag the structure with the mouse to rotate
, resolution 2.25Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN


Overview

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.

About this Structure

1P32 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein., Jiang J, Zhang Y, Krainer AR, Xu RM, Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3572-7. PMID:10097078

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