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PDBsum entry 5k3j
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Oxidoreductase
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PDB id
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5k3j
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystals structure of acyl-coa oxidase-2 in caenorhabditis elegans bound with fad, ascaroside-coa, and atp
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Structure:
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Acyl-coenzyme a oxidase. Chain: a, b. Engineered: yes. Mutation: yes
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Source:
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Caenorhabditis elegans. Organism_taxid: 6239. Gene: acox-2, cele_f08a8.2, f08a8.2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.68Å
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R-factor:
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0.215
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R-free:
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0.245
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Authors:
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X.Zhang,K.Li,R.A.Jones,S.D.Bruner,R.A.Butcher
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Key ref:
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X.Zhang
et al.
(2016).
Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
Proc Natl Acad Sci U S A,
113,
10055-10060.
PubMed id:
DOI:
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Date:
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19-May-16
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Release date:
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24-Aug-16
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PROCHECK
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Headers
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References
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O62137
(O62137_CAEEL) -
Acyl-coenzyme A oxidase acox-1.2 from Caenorhabditis elegans
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Seq:
Struc:
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661 a.a.
662 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Proc Natl Acad Sci U S A
113:10055-10060
(2016)
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PubMed id:
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Structural characterization of acyl-CoA oxidases reveals a direct link between pheromone biosynthesis and metabolic state in Caenorhabditis elegans.
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X.Zhang,
K.Li,
R.A.Jones,
S.D.Bruner,
R.A.Butcher.
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ABSTRACT
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Caenorhabditis elegans secretes ascarosides as pheromones to communicate with
other worms and to coordinate the development and behavior of the population.
Peroxisomal β-oxidation cycles shorten the side chains of ascaroside precursors
to produce the short-chain ascaroside pheromones. Acyl-CoA oxidases, which
catalyze the first step in these β-oxidation cycles, have different side
chain-length specificities and enable C. elegans to regulate the production of
specific ascaroside pheromones. Here, we determine the crystal structure of the
acyl-CoA oxidase 1 (ACOX-1) homodimer and the ACOX-2 homodimer bound to its
substrate. Our results provide a molecular basis for the substrate specificities
of the acyl-CoA oxidases and reveal why some of these enzymes have a very broad
substrate range, whereas others are quite specific. Our results also enable
predictions to be made for the roles of uncharacterized acyl-CoA oxidases in C.
elegans and in other nematode species. Remarkably, we show that most of the C.
elegans acyl-CoA oxidases that participate in ascaroside biosynthesis contain a
conserved ATP-binding pocket that lies at the dimer interface, and we identify
key residues in this binding pocket. ATP binding induces a structural change
that is associated with tighter binding of the FAD cofactor. Mutations that
disrupt ATP binding reduce FAD binding and reduce enzyme activity. Thus, ATP may
serve as a regulator of acyl-CoA oxidase activity, thereby directly linking
ascaroside biosynthesis to ATP concentration and metabolic state.
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Links
