 |
PDBsum entry 3ku2
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transferase
|
|
|
Title:
|
|
Crystal structure of inactivated form of cdpk1 from toxoplasma gondii, tgme49.101440
|
|
Structure:
|
|
Calmodulin-domain protein kinase 1. Chain: a. Engineered: yes
|
|
Source:
|
|
Toxoplasma gondii. Organism_taxid: 5811. Gene: cdpk1, tgme49_101440. Expressed in: escherichia coli. Expression_system_taxid: 562
|
|
Resolution:
|
|
|
2.30Å
|
R-factor:
|
0.198
|
R-free:
|
0.237
|
|
|
Authors:
|
|
A.K.Wernimont,J.D.Artz,P.Finnerty,T.Xiao,H.He,F.Mackenzie, G.Sinestera,A.A.Hassani,G.Wasney,M.Vedadi,S.Lourido,A.Bochkarev, C.H.Arrowsmith,A.M.Edwards,C.Bountra,J.Weigelt,D.L.Sibley,R.Hui, Y.H.Lin,Structural Genomics Consortium (Sgc)
|
|
Key ref:
|
|
A.K.Wernimont
et al.
(2010).
Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.
Nat Struct Biol,
17,
596-601.
PubMed id:
|
|
|
Date:
|
|
|
26-Nov-09
|
Release date:
|
16-Feb-10
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q9BJF5
(Q9BJF5_TOXGO) -
Calmodulin-domain protein kinase 1 from Toxoplasma gondii
|
|
|
|
Seq:
Struc:
|
|
|
|
507 a.a.
457 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Nat Struct Biol
17:596-601
(2010)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.
|
|
A.K.Wernimont,
J.D.Artz,
P.Finerty,
Y.H.Lin,
M.Amani,
A.Allali-Hassani,
G.Senisterra,
M.Vedadi,
W.Tempel,
F.Mackenzie,
I.Chau,
S.Lourido,
L.D.Sibley,
R.Hui.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Calcium-dependent protein kinases (CDPKs) have pivotal roles in the
calcium-signaling pathway in plants, ciliates and apicomplexan parasites and
comprise a calmodulin-dependent kinase (CaMK)-like kinase domain regulated by a
calcium-binding domain in the C terminus. To understand this intramolecular
mechanism of activation, we solved the structures of the autoinhibited (apo) and
activated (calcium-bound) conformations of CDPKs from the apicomplexan parasites
Toxoplasma gondii and Cryptosporidium parvum. In the apo form, the C-terminal
CDPK activation domain (CAD) resembles a calmodulin protein with an unexpected
long helix in the N terminus that inhibits the kinase domain in the same manner
as CaMKII. Calcium binding triggers the reorganization of the CAD into a highly
intricate fold, leading to its relocation around the base of the kinase domain
to a site remote from the substrate binding site. This large conformational
change constitutes a distinct mechanism in calcium signal-transduction pathways.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
A.K.Wernimont,
M.Amani,
W.Qiu,
J.C.Pizarro,
J.D.Artz,
Y.H.Lin,
J.Lew,
A.Hutchinson,
and
R.Hui
(2011).
Structures of parasitic CDPK domains point to a common mechanism of activation.
|
| |
Proteins,
79,
803-820.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
S.Franz,
B.Ehlert,
A.Liese,
J.Kurth,
A.C.Cazalé,
and
T.Romeis
(2011).
Calcium-dependent protein kinase CPK21 functions in abiotic stress response in Arabidopsis thaliana.
|
| |
Mol Plant,
4,
83-96.
|
|
|
|
|
|
|
C.Doerig,
and
O.Billker
(2010).
A parasite calcium switch and Achilles' heel revealed.
|
| |
Nat Struct Mol Biol,
17,
541-543.
|
|
|
|
|
|
|
L.D.Sibley
(2010).
How apicomplexan parasites move in and out of cells.
|
| |
Curr Opin Biotechnol,
21,
592-598.
|
|
|
|
|
|
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.
|
|
Links
