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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >2.4 angstrom resolution crystal structure of human TRAP1(NM), the Hsp90 paralog in the mitochondrial matrix
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2.4 angstrom resolution crystal structure of human TRAP1(NM), the Hsp90 paralog in the mitochondrial matrix

机译：2.4埃分辨率晶体结构的人类TRAP1 (NM),一半在线粒体假字矩阵

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摘要

TRAP1 is an organelle-specific Hsp90 paralog that is essential for neoplastic growth. As a member of the Hsp90 family, TRAP1 is presumed to be a general chaperone facilitating the late-stage folding of Hsp90 client proteins in the mitochondrial matrix. Interestingly, TRAP1 cannot replace cytosolic Hsp90 in protein folding, and none of the known Hsp90 co-chaperones are found in mitochondria. Thus, the three-dimensional structure of TRAP1 must feature regulatory elements that are essential to the ATPase activity and chaperone function of TRAP1. Here, the crystal structure of a human TRAP1(NM) dimer is presented, featuring an intact N-domain and M-domain structure, bound to adenosine 5'-beta,gamma-imidotriphosphate (ADPNP). The crystal structure together with epitope-mapping results shows that the TRAP1 M-domain loop 1 contacts the neighboring subunit and forms a previously unobserved third dimer interface that mediates the specific interaction with mitochondrial Hsp70.
机译：TRAP1是organelle-specific一半假字对肿瘤增长至关重要。一半的家庭,TRAP1原本作为一个一般伴护方便后期一半端蛋白质的折叠线粒体基质。在蛋白质折叠一半寿命取代胞质,没有已知的一半co-chaperones被发现在线粒体。TRAP1必须功能监管的结构腺苷三磷酸酶的元素是必不可少的活动和女伴TRAP1的函数。人类的晶体结构TRAP1 (NM)二聚体,一个完整的N-domain和M-domain结构、腺苷5“-beta, gamma-imidotriphosphate (ADPNP)。晶体结构与epitope-mapping一起结果表明,TRAP1 M-domain循环1联系人邻近单元和形式以前第三二聚体界面介导的特定相互作用线粒体Hsp70。

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