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PDBsum entry 5ein
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Oxidoreductase/biosynthetic protein
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PDB id
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5ein
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the lysy·lysw complex from thermus thermophilus.
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Authors
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T.Shimizu,
T.Tomita,
T.Kuzuyama,
M.Nishiyama.
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Ref.
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J Biol Chem, 2016,
291,
9948-9959.
[DOI no: ]
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PubMed id
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Abstract
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Several bacteria and archaea utilize the amino group-carrier protein, LysW, for
lysine biosynthesis, in which an isopeptide bond is formed between the
C-terminal Glu of LysW and an amino group of α-aminoadipate (AAA). The
resulting LysW-γ-AAA is phosphorylated by LysZ to form LysW-γ-AAA phosphate,
which is subsequently reduced to LysW-γ-aminoadipic semialdehyde (LysW-γ-AASA)
through a reaction catalyzed by LysY. In this study, we determined the crystal
structures of LysY from Thermus thermophilus HB27 (TtLysY) complexed with
TtLysW-γ-AASA and TtLysW-γ-AAA, respectively. In both structures, the globular
domain of TtLysW was recognized by positively charged residues on helix α9 and
the β11-α10 loop of TtLysY through conformational changes. A mutational
analysis confirmed that the interactions observed between TtLysY and TtLysW are
important for the function of TtLysY. The extended LysW recognition loop and
conserved arginine residue were identified as signatures to discriminate LysY
from ArgC, which is involved in arginine biosynthesis. Combined with the
previously determined TtLysZ·TtLysW complex structure, TtLysW may
simultaneously bind TtLysZ and TtLysY. These structural insights suggest the
formation of a TtLysWZY ternary complex, in which the flexible C-terminal
extension of TtLysW promotes the efficient transfer of the labile intermediate
from the active site of TtLysZ to that of TtLysY during the sequential reactions
catalyzed by TtLysZY.
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