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PDBsum entry 4l1l
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PDB id:
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Transferase
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Title:
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Rat pkc c2 domain bound to cd
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Structure:
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Protein kinasE C alpha type. Chain: a. Fragment: unp residues 155-293. Synonym: pkc-a, pkc-alpha. Engineered: yes
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: pkca, prkca. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.60Å
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R-factor:
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0.160
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R-free:
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0.195
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Authors:
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K.M.Morales,Y.Yang,Z.Long,P.Li,A.B.Taylor,P.J.Hart,T.I.Igumenova
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Key ref:
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K.A.Morales
et al.
(2013).
Cd2+ as a Ca2+ surrogate in protein-membrane interactions: isostructural but not isofunctional.
J Am Chem Soc,
135,
12980-12983.
PubMed id:
DOI:
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Date:
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03-Jun-13
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Release date:
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28-Aug-13
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PROCHECK
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Headers
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References
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P05696
(KPCA_RAT) -
Protein kinase C alpha type from Rattus norvegicus
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Seq:
Struc:
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672 a.a.
138 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.11.13
- protein kinase C.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Am Chem Soc
135:12980-12983
(2013)
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PubMed id:
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Cd2+ as a Ca2+ surrogate in protein-membrane interactions: isostructural but not isofunctional.
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K.A.Morales,
Y.Yang,
Z.Long,
P.Li,
A.B.Taylor,
P.J.Hart,
T.I.Igumenova.
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ABSTRACT
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Due to its favorable spectroscopic properties, Cd(2+) is frequently used as a
probe of Ca(2+) sites in proteins. We investigate the ability of Cd(2+) to act
as a structural and functional surrogate of Ca(2+) in protein-membrane
interactions. C2 domain from protein kinase Cα (C2α) was chosen as a paradigm
for the Ca(2+)-dependent phosphatidylserine-binding peripheral membrane domains.
We identified the Cd(2+)-binding sites of C2α using NMR spectroscopy,
determined the 1.6 Å crystal structure of Cd(2+)-bound C2α, and characterized
metal-ion-dependent interactions between C2α and phospholipid membranes using
fluorescence spectroscopy and ultracentrifugation experiments. We show that
Cd(2+) forms a tight complex with the membrane-binding loops of C2α but is
unable to support its membrane-binding function. This is in sharp contrast with
Pb(2+), which is almost as effective as Ca(2+) in driving the C2α-membrane
association process. Our results provide the first direct evidence for the
specific role of divalent metal ions in mediating protein-membrane interactions,
have important implications for metal substitution studies in proteins, and
illustrate the potential diversity of functional responses caused by toxic metal
ions.
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Links
