Self-assembly of glutathione S-transferase into nanowires.
This study presents the Ni-ion-directed self-assembly of a C(2)-symmetric homodimeric enzyme into nanowires. A genetically introduced His-tag arm stretches out of the central structure of a C(2)-symmetric homodimer of glutathione S-transferase, which is used as a linker to recruit a second building block through interprotein metal coordination, forming self-assembled one-dimensional nanostructures with excellent enzymatic activity.
State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, 2699 Qianjin Road, Changchun 130012, China.
Wei
W
Zhang
Quan
Q
Luo
Lu
L
Miao
Chunxi
C
Hou
Yushi
Y
Bai
Zeyuan
Z
Dong
Jiayun
J
Xu
Junqiu
J
Liu
D002942:Circular Dichroism; D019281:Dimerization; D004492:Edetic Acid / Q000737:chemistry; D005982:Glutathione Transferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006639:Histidine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007477:Ions / Q000737:chemistry; D053770:Nanowires / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
C471213:His-His-His-His-His-His; D007477:Ions; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D006639:Histidine; D009532:Nickel; D004492:Edetic Acid; D005982:Glutathione Transferase