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人p32的晶体结构,一种呈甜甜圈状的酸性线粒体基质蛋白。

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

作者信息

Jiang J, Zhang Y, Krainer A R, Xu R M

机构信息

W. M. Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.

出版信息

Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3572-7. doi: 10.1073/pnas.96.7.3572.

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.

摘要

人类p32蛋白(也称为SF2相关p32、p32/TAP和gC1qR)是一种保守的真核蛋白,主要定位于线粒体基质中。它被认为参与线粒体氧化磷酸化以及细胞核与线粒体的相互作用。我们报道了分辨率为2.25埃的p32晶体结构。该结构显示,p32呈现出一种新颖的折叠结构,具有七个连续的反平行β链,两侧分别是一个N端α螺旋和两个C端α螺旋。三个单体形成一个甜甜圈形状的四级结构,其表面电荷分布异常不对称。本文讨论了该结构对先前提出的p32功能的影响,并提出了新的特定功能特性。

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