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Chaperones metal transfer mechanism

The Hahl structures provide insight into the molecular mechanism of metal transfer between the Atxl-like chaperones and their partner ATPases. The target proteins of Hahl are the Menkes and Wilson disease proteins (Section 8.8.2.1). In the Cu Hahl structure, the coordination geometry is distorted tetrahedral with three Cu "S distances of 2.3 A and the fourth sulfur at... [Pg.197]

Based on the wealth of both in vivo and in vitro biochemical experiments described in Section II, A, a diffusion-driven or bucket brigade mechanism of metal ion transfer between MXCXXC-motifs on the copper chaperone proteins and their target domains was predicted (Pufahl et al.. [Pg.177]

These coordination geometries are consistent with a proposed mechanism in which the metal ion is transferred from chaperone to target protein by the formation of two- and three-coordinate... [Pg.197]


See other pages where Chaperones metal transfer mechanism is mentioned: [Pg.180]    [Pg.318]    [Pg.319]    [Pg.179]    [Pg.208]    [Pg.316]    [Pg.107]    [Pg.165]    [Pg.178]    [Pg.138]    [Pg.491]   
See also in sourсe #XX -- [ Pg.177 , Pg.178 , Pg.209 ]




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