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1p32

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[[Image:1p32.gif|left|200px]]
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{{STRUCTURE_1p32| PDB=1p32 | SCENE= }}
{{STRUCTURE_1p32| PDB=1p32 | SCENE= }}
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'''CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN'''
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===CRYSTAL STRUCTURE OF HUMAN P32, A DOUGHNUT-SHAPED ACIDIC MITOCHONDRIAL MATRIX PROTEIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10097078 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10097078}}
==About this Structure==
==About this Structure==
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[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
[[Category: Mitochondrial matrix protein]]
[[Category: Mitochondrial matrix protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:37:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:41:31 2008''

Revision as of 12:41, 27 July 2008

Image:1p32.png

Template:STRUCTURE 1p32

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

Template:ABSTRACT PUBMED 10097078

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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