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PDBsum entry 6uxh
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Plant protein, transferase
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PDB id
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6uxh
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References listed in PDB file
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Key reference
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Title
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Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.
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Authors
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D.A.Korasick,
P.K.Kandoth,
J.J.Tanner,
M.G.Mitchum,
L.J.Beamer.
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Ref.
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J Biol Chem, 2020,
295,
3708-3718.
[DOI no: ]
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PubMed id
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Abstract
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Management of the agricultural pathogen soybean cyst nematode (SCN) relies on
the use of SCN-resistant soybean cultivars, a strategy that has been failing in
recent years. An underutilized source of resistance in the soybean genotype
Peking is linked to two polymorphisms in serine hydroxy-methyltransferase 8
(SHMT8). SHMT is a pyridoxal 5'-phosphate-dependent enzyme that converts
l-serine and (6S)-tetrahydrofolate to glycine and
5,10-methylenetetrahydrofolate. Here, we determined five crystal structures of
the 1884-residue SHMT8 tetramers from the SCN-susceptible cultivar (cv.) Essex
and the SCN-resistant cv. Forrest (whose resistance is derived from the SHMT8
polymorphisms in Peking); the crystal structures were determined in complex with
various ligands at 1.4-2.35 Å resolutions. We find that the two
Forrest-specific polymorphic substitutions (P130R and N358Y) impact the mobility
of a loop near the entrance of the (6S)-tetrahydrofolate-binding site.
Ligand-binding and kinetic studies indicate severely reduced affinity for folate
and dramatically impaired enzyme activity in Forrest SHMT8. These findings imply
widespread effects on folate metabolism in soybean cv. Forrest that have
implications for combating the widespread increase in virulent SCN.
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