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PDBsum entry 3vpc
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PDB id:
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Ligase
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Title:
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Argx from sulfolobus tokodaii complexed with adp
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Structure:
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Putative acetylornithine deacetylase. Chain: a, b, c, d. Synonym: stargx. Engineered: yes
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Source:
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Sulfolobus tokodaii. Organism_taxid: 111955. Strain: dsm 16993, jcm 10545, nbrc 100140, 7. Gene: argx. Expressed in: escherichia coli. Expression_system_taxid: 273063.
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Resolution:
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1.87Å
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R-factor:
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0.201
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R-free:
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0.253
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Authors:
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T.Tomita,A.Horie,T.Kuzuyama,M.Nishiyama
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Key ref:
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T.Ouchi
et al.
(2013).
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
Nat Chem Biol,
9,
277-283.
PubMed id:
DOI:
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Date:
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29-Feb-12
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Release date:
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27-Feb-13
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PROCHECK
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Headers
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References
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Q970U6
(ARGX_SULTO) -
Glutamate--LysW ligase ArgX from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
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Seq:
Struc:
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282 a.a.
282 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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DOI no:
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Nat Chem Biol
9:277-283
(2013)
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PubMed id:
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Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
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T.Ouchi,
T.Tomita,
A.Horie,
A.Yoshida,
K.Takahashi,
H.Nishida,
K.Lassak,
H.Taka,
R.Mineki,
T.Fujimura,
S.Kosono,
C.Nishiyama,
R.Masui,
S.Kuramitsu,
S.V.Albers,
T.Kuzuyama,
M.Nishiyama.
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ABSTRACT
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LysW has been identified as a carrier protein in the lysine biosynthetic pathway
that is active through the conversion of α-aminoadipate (AAA) to lysine. In
this study, we found that the hyperthermophilic archaeon, Sulfolobus
acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection
of AAA but also uses LysW to protect the amino group of glutamate in arginine
biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are
converted to lysine and ornithine, respectively, by a single set of enzymes with
dual functions. The crystal structure of ArgX, the enzyme responsible for
modification and protection of the amino moiety of glutamate with LysW, was
determined in complex with LysW. Structural comparison and enzymatic
characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX
identify the amino acid motif responsible for substrate discrimination between
AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at
different stages of evolution led to ArgX and LysX.
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