 |
PDBsum entry 1gcb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
DNA binding protein
|
PDB id
|
|
|
|
1gcb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6.
|
|
|
Authors
|
|
L.Joshua-Tor,
H.E.Xu,
S.A.Johnston,
D.C.Rees.
|
|
|
Ref.
|
|
Science, 1995,
269,
945-950.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
78%.
|
|
|
|
Abstract
|
|
|
Bleomycin hydrolase is a cysteine protease that hydrolyzes the anticancer drug
bleomycin. The homolog in yeast, Gal6, has recently been identified and found to
bind DNA and to act as a repressor in the Gal4 regulatory system. The crystal
structure of Gal6 at 2.2 A resolution reveals a hexameric structure with a
prominent central channel. The papain-like active sites are situated within the
central channel, in a manner resembling the organization of active sites in the
proteasome. The Gal6 channel is lined with 60 lysine residues from the six
subunits, suggesting a role in DNA binding. The carboxyl-terminal arm of Gal6
extends into the active site cleft and may serve a regulatory function. Rather
than each residing in distinct, separable domains, the protease and DNA-binding
activities appear structurally intertwined in the hexamer, implying a coupling
of these two activities.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Yeast bleomycin hydrolase is a DNA-Binding cysteine protease. Identification, Purification, Biochemical characterization.
|
|
|
Authors
|
|
H.E.Xu,
S.A.Johnston.
|
|
|
Ref.
|
|
J Biol Chem, 1994,
269,
21177-21183.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
