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PDBsum entry 2kui
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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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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Structure
18:606-615
(2010)
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PubMed id:
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The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation.
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P.Barthe,
G.V.Mukamolova,
C.Roumestand,
M.Cohen-Gonsaud.
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ABSTRACT
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PknB is a transmembrane Ser/Thr protein kinase that defines and belongs to an
ultraconserved kinase subfamily found in Gram-positive bacteria. Essential for
Mycobacterium tuberculosis growth, its close homolog in Bacillus subtilis has
been linked to exit from dormancy. The kinase possesses an extracellular region
composed of a repetition of PASTA domains, believed to bind peptidoglycan
fragments that might act as a signaling molecule. We report here the first
solution structure of this extracellular region. Small-angle X-ray scattering
and nuclear magnetic resonance studies show that the four PASTA domains display
an unexpected linear organization, contrary to what is observed in the distant
protein PBP2x from Streptococccus pneumoniae where two PASTA domains fold over
in a compact structure. We propose a model for PknB activation based on a
ligand-dependent dimerization of the extracellular PASTA domains that initiates
multiple signaling pathways.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Ruggiero,
F.Squeglia,
D.Marasco,
R.Marchetti,
A.Molinaro,
and
R.Berisio
(2011).
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
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Biochem J,
435,
33-41.
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PDB code:
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G.Jones,
R.Del Sol,
E.Dudley,
and
P.Dyson
(2011).
Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.
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Microb Biotechnol,
4,
263-274.
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T.N.Lombana,
N.Echols,
M.C.Good,
N.D.Thomsen,
H.L.Ng,
A.E.Greenstein,
A.M.Falick,
D.S.King,
and
T.Alber
(2010).
Allosteric activation mechanism of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknB.
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Structure,
18,
1667-1677.
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V.Molle,
G.Gulten,
C.Vilchèze,
R.Veyron-Churlet,
I.Zanella-Cléon,
J.C.Sacchettini,
W.R.Jacobs,
and
L.Kremer
(2010).
Phosphorylation of InhA inhibits mycolic acid biosynthesis and growth of Mycobacterium tuberculosis.
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Mol Microbiol,
78,
1591-1605.
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PDB codes:
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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.
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Links
