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PDBsum entry 4xl2
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PDB id:
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Transferase
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Title:
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Crystal structure of oxidized form of thiolase from clostridium acetobutylicum
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Structure:
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Acetyl-coa acetyltransferase. Chain: a, b. Synonym: acetoacetyl-coa thiolase. Engineered: yes
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Source:
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Clostridium acetobutylicum (strain atcc 824 / dsm 792 / jcm 1419 / lmg 5710 / vkm b-1787). Organism_taxid: 272562. Strain: atcc 824 / dsm 792 / jcm 1419 / lmg 5710 / vkm b-1787. Gene: thla, thl, ca_c2873. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.77Å
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R-factor:
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0.157
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R-free:
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0.191
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Authors:
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S.Kim,S.C.Ha,J.W.Ahn,E.J.Kim,J.H.Lim,K.J.Kim
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Key ref:
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S.Kim
et al.
(2015).
Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.
Nat Commun,
6,
8410.
PubMed id:
DOI:
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Date:
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13-Jan-15
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Release date:
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07-Oct-15
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PROCHECK
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Headers
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References
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P45359
(THLA_CLOAB) -
Acetyl-CoA acetyltransferase from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
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Seq:
Struc:
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392 a.a.
384 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.2.3.1.9
- acetyl-CoA C-acetyltransferase.
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Pathway:
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Mevalonate Biosynthesis
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Reaction:
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2 acetyl-CoA = acetoacetyl-CoA + CoA
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2
×
acetyl-CoA
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=
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acetoacetyl-CoA
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+
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CoA
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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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Nat Commun
6:8410
(2015)
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PubMed id:
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Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.
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S.Kim,
Y.S.Jang,
S.C.Ha,
J.W.Ahn,
E.J.Kim,
J.H.Lim,
C.Cho,
Y.S.Ryu,
S.K.Lee,
S.Y.Lee,
K.J.Kim.
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ABSTRACT
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Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme
A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the
biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate
the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its
reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as
Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch
modulation through reversible disulfide bond formation between two catalytic
cysteine residues, Cys88 and Cys378. When CaTHL is overexpressed in wild-type C.
acetobutylicum, butanol production is reduced due to the disturbance of
acidogenic to solventogenic shift. The CaTHL(V77Q/N153Y/A286K) mutant, which is
not able to form disulfide bonds, exhibits higher activity than wild-type CaTHL,
and enhances butanol production upon overexpression. On the basis of these
results, we suggest that CaTHL functions as a key enzyme in the regulation of
the main metabolism of C. acetobutylicum through a redox-switch regulatory
mechanism.
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