 |
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Hydrolase, apoptosis
|
PDB id
|
|
|
|
3cm5
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Cellular component
|
intracellular
|
1 term
|
 |
|
Biochemical function
|
nucleic acid binding
|
2 terms
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Mol Cell Biol
29:448-457
(2009)
|
|
PubMed id:
|
|
|
|
|
| |
|
Crystal structure of CRN-4: implications for domain function in apoptotic DNA degradation.
|
|
Y.Y.Hsiao,
A.Nakagawa,
Z.Shi,
S.Mitani,
D.Xue,
H.S.Yuan.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
Cell death related nuclease 4 (CRN-4) is one of the apoptotic nucleases involved
in DNA degradation in Caenorhabditis elegans. To understand how CRN-4 is
involved in apoptotic DNA fragmentation, we analyzed CRN-4's biochemical
properties, in vivo cell functions, and the crystal structures of CRN-4 in
apo-form, Mn(2+)-bound active form, and Er(3+)-bound inactive form. CRN-4 is a
dimeric nuclease with the optimal enzyme activity in cleaving double-stranded
DNA in apoptotic salt conditions. Both mutational studies and the structures of
the Mn(2+)-bound CRN-4 revealed the geometry of the functional nuclease active
site in the N-terminal DEDDh domain. The C-terminal domain, termed the
Zn-domain, contains basic surface residues ideal for nucleic acid recognition
and is involved in DNA binding, as confirmed by deletion assays. Cell death
analysis in C. elegans further demonstrated that both the nuclease active site
and the Zn-domain are required for crn-4's function in apoptosis. Combining all
of the data, we suggest a structural model where chromosomal DNA is bound at the
Zn-domain and cleaved at the DEDDh nuclease domain in CRN-4 when the cell is
undergoing apoptosis.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
K.M.Hastie,
C.R.Kimberlin,
M.A.Zandonatti,
I.J.MacRae,
and
E.O.Saphire
(2011).
Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression.
|
| |
Proc Natl Acad Sci U S A, 108,
2396-2401.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
W.Yang
(2011).
Nucleases: diversity of structure, function and mechanism.
|
| |
Q Rev Biophys, 44,
1.
|
 |
|
|
|
|
 |
Y.Y.Hsiao,
C.C.Yang,
C.L.Lin,
J.L.Lin,
Y.Duh,
and
H.S.Yuan
(2011).
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation.
|
| |
Nat Chem Biol, 7,
236-243.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
C.C.Yang,
Y.T.Wang,
Y.Y.Hsiao,
L.G.Doudeva,
P.H.Kuo,
S.Y.Chow,
and
H.S.Yuan
(2010).
Structural and biochemical characterization of CRN-5 and Rrp46: an exosome component participating in apoptotic DNA degradation.
|
| |
RNA, 16,
1748-1759.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
B.He,
N.Lu,
and
Z.Zhou
(2009).
Cellular and nuclear degradation during apoptosis.
|
| |
Curr Opin Cell Biol, 21,
900-912.
|
 |
|
 |
 |
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
|