 |
PDBsum entry 1m39
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Biochemistry
42:1439-1450
(2003)
|
|
PubMed id:
|
|
|
|
|
| |
|
C-terminal half of human centrin 2 behaves like a regulatory EF-hand domain.
|
|
E.Matei,
S.Miron,
Y.Blouquit,
P.Duchambon,
I.Durussel,
J.A.Cox,
C.T.Craescu.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the
centrosome duplication and separation during cell division. We studied the
structural and Ca(2+)-binding properties of two C-terminal fragments of this
protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172),
having 10 additional residues. Both fragments are highly disordered in the apo
state but become better structured (although not conformationally homogeneous)
in the presence of Ca(2+) and depending on the nature of the cations (K(+) or
Na(+)) in the buffer. Only the longer C-terminal domain, in the Ca(2+)-saturated
state and in the presence of Na(+) ions, was amenable to structure determination
by nuclear magnetic resonance. The solution structure of LC-HsCen2 reveals an
open two EF-hand structure, similar to the conformation of related
Ca(2+)-saturated regulatory domains. Unexpectedly, the N-terminal helix segment
(F86-T94) lies over the exposed hydrophobic cavity. This unusual intramolecular
interaction increases considerably the Ca(2+) affinity and constitutes a useful
model for the target binding.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
K.K.Resendes,
B.A.Rasala,
and
D.J.Forbes
(2008).
Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export.
|
| |
Mol Cell Biol,
28,
1755-1769.
|
 |
|
|
|
|
 |
P.Trojan,
N.Krauss,
H.W.Choe,
A.Giessl,
A.Pulvermüller,
and
U.Wolfrum
(2008).
Centrins in retinal photoreceptor cells: regulators in the connecting cilium.
|
| |
Prog Retin Eye Res,
27,
237-259.
|
 |
|
|
|
|
 |
Y.Blouquit,
P.Duchambon,
E.Brun,
S.Marco,
F.Rusconi,
and
C.Sicard-Roselli
(2007).
High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target.
|
| |
Free Radic Biol Med,
43,
216-228.
|
 |
|
|
|
|
 |
J.B.Charbonnier,
P.Christova,
A.Shosheva,
E.Stura,
M.H.Le Du,
Y.Blouquit,
P.Duchambon,
S.Miron,
and
C.T.Craescu
(2006).
Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
649-651.
|
 |
|
|
|
|
 |
J.H.Sheehan,
C.G.Bunick,
H.Hu,
P.A.Fagan,
S.M.Meyn,
and
W.J.Chazin
(2006).
Structure of the N-terminal calcium sensor domain of centrin reveals the biochemical basis for domain-specific function.
|
| |
J Biol Chem,
281,
2876-2881.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
J.Martinez-Sanz,
A.Yang,
Y.Blouquit,
P.Duchambon,
L.Assairi,
and
C.T.Craescu
(2006).
Binding of human centrin 2 to the centrosomal protein hSfi1.
|
| |
FEBS J,
273,
4504-4515.
|
 |
|
|
|
|
 |
J.R.Thompson,
Z.C.Ryan,
J.L.Salisbury,
and
R.Kumar
(2006).
The structure of the human centrin 2-xeroderma pigmentosum group C protein complex.
|
| |
J Biol Chem,
281,
18746-18752.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
L.Liang,
S.Flury,
V.Kalck,
B.Hohn,
and
J.Molinier
(2006).
CENTRIN2 interacts with the Arabidopsis homolog of the human XPC protein (AtRAD4) and contributes to efficient synthesis-dependent repair of bulky DNA lesions.
|
| |
Plant Mol Biol,
61,
345-356.
|
 |
|
|
|
|
 |
T.A.Craig,
L.M.Benson,
H.R.Bergen,
S.Y.Venyaminov,
J.L.Salisbury,
Z.C.Ryan,
J.R.Thompson,
J.Sperry,
M.L.Gross,
and
R.Kumar
(2006).
Metal-binding properties of human centrin-2 determined by micro-electrospray ionization mass spectrometry and UV spectroscopy.
|
| |
J Am Soc Mass Spectrom,
17,
1158-1171.
|
 |
|
|
|
|
 |
J.H.Park,
N.Krauss,
A.Pulvermüller,
P.Scheerer,
W.Höhne,
A.Giessl,
U.Wolfrum,
K.P.Hofmann,
O.P.Ernst,
and
H.W.Choe
(2005).
Crystallization and preliminary X-ray studies of mouse centrin1.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
510-513.
|
 |
|
|
|
|
 |
R.Nishi,
Y.Okuda,
E.Watanabe,
T.Mori,
S.Iwai,
C.Masutani,
K.Sugasawa,
and
F.Hanaoka
(2005).
Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.
|
| |
Mol Cell Biol,
25,
5664-5674.
|
 |
|
|
|
|
 |
S.Geimer,
and
M.Melkonian
(2005).
Centrin scaffold in Chlamydomonas reinhardtii revealed by immunoelectron microscopy.
|
| |
Eukaryot Cell,
4,
1253-1263.
|
 |
|
|
|
|
 |
J.L.Salisbury
(2004).
Centrosomes: Sfi1p and centrin unravel a structural riddle.
|
| |
Curr Biol,
14,
R27-R29.
|
 |
|
|
|
|
 |
M.Tourbez,
C.Firanescu,
A.Yang,
L.Unipan,
P.Duchambon,
Y.Blouquit,
and
C.T.Craescu
(2004).
Calcium-dependent self-assembly of human centrin 2.
|
| |
J Biol Chem,
279,
47672-47680.
|
 |
|
|
|
|
 |
A.Popescu,
S.Miron,
Y.Blouquit,
P.Duchambon,
P.Christova,
and
C.T.Craescu
(2003).
Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin.
|
| |
J Biol Chem,
278,
40252-40261.
|
 |
|
 |
 |
|
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
code is
shown on the right.
|
');
}
}
 |