期刊
STRUCTURE
卷 17, 期 5, 页码 749-758出版社
CELL PRESS
DOI: 10.1016/j.str.2009.03.005
关键词
-
资金
- NCRR NIH HHS [P41 RR002250, P41 RR002250-23, P41 RR02250, P41 RR002250-22, P41 RR002250-24] Funding Source: Medline
- NEI NIH HHS [2 PN2 EY016525, PN2 EY016525, PN2 EY016525-04, PN1 EY016525, PN2 EY016525-03, PN1 EY016525-01, PN2 EY016525-02] Funding Source: Medline
- NIGMS NIH HHS [R01 GM08139, R01 GM080139-03, R01 GM080139] Funding Source: Medline
Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in each subunit, exposing the entrance to the active site; this movement is stabilized by enhanced interhexamer and interdodecamer interactions, particularly in the central linker subunits. This mechanism could be applicable to other type 3 copper proteins, as the active site is highly conserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据