1p32
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(New page: 200px<br /> <applet load="1p32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p32, resolution 2.25Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:33, 12 November 2007
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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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