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PDBsum entry 4jax
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PDB id:
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Transferase
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Title:
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Crystal structure of dimeric klhxk1 in crystal form x
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Structure:
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Hexokinase. Chain: a, b, c, d, e, f. Engineered: yes
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Source:
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Kluyveromyces lactis. Yeast. Organism_taxid: 284590. Strain: cbs2359/152. Gene: klla0d11352g, rag5. Expressed in: kluyveromyces lactis. Expression_system_taxid: 28985.
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Resolution:
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2.26Å
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R-factor:
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0.201
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R-free:
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0.240
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Authors:
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E.B.Kuettner,N.Strater,K.Kettner,A.Otto,H.Lilie,R.P.Golbik, T.M.Kriegel
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Key ref:
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K.Kettner
et al.
(2013).
In vivo phosphorylation and in vitro autophosphorylation-inactivation of Kluyveromyces lactis hexokinase KlHxk1.
Biochem Biophys Res Commun,
435,
313-318.
PubMed id:
DOI:
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Date:
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19-Feb-13
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Release date:
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01-May-13
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PROCHECK
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Headers
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References
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P33284
(HXK_KLULA) -
Hexokinase from Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
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Seq:
Struc:
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485 a.a.
470 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.2.7.1.1
- hexokinase.
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Reaction:
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a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H+
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D-hexose
Bound ligand (Het Group name = )
matches with 50.00% similarity
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ATP
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=
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D-hexose 6-phosphate
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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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Biochem Biophys Res Commun
435:313-318
(2013)
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PubMed id:
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In vivo phosphorylation and in vitro autophosphorylation-inactivation of Kluyveromyces lactis hexokinase KlHxk1.
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K.Kettner,
E.B.Kuettner,
A.Otto,
H.Lilie,
R.P.Golbik,
N.Sträter,
T.M.Kriegel.
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ABSTRACT
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The bifunctional hexokinase KlHxk1 is a key component of glucose-dependent
signal transduction in Kluyveromyces lactis. KlHxk1 is phosphorylated in vivo
and undergoes ATP-dependent autophosphorylation-inactivation in vitro. This
study identifies serine-15 as the site of in vivo phosphorylation and serine-157
as the autophosphorylation-inactivation site. X-ray crystallography of the in
vivo phosphorylated enzyme indicates the existence of a ring-shaped symmetrical
homodimer carrying two phosphoserine-15 residues. In contrast, small-angle X-ray
scattering and equilibrium sedimentation analyses reveal the existence of
monomeric phosphoserine-15 KlHxk1 in solution. While phosphorylation at
serine-15 and concomitant homodimer dissociation are likely to be involved in
glucose signalling, mechanism and putative physiological significance of KlHxk1
inactivation by autophosphorylation at serine-157 remain to be established.
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