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PDBsum entry 3u3d
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References listed in PDB file
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Key reference
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Title
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Plasmodium falciparum sir2a preferentially hydrolyzes medium and long chain fatty acyl lysine.
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Authors
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A.Y.Zhu,
Y.Zhou,
S.Khan,
K.W.Deitsch,
Q.Hao,
H.Lin.
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Ref.
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Acs Chem Biol, 2012,
7,
155-159.
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PubMed id
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Abstract
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Plasmodium falciparum Sir2A (PfSir2A), a member of the sirtuin family of
nicotinamide adenine dinucleotide-dependent deacetylases, has been shown to
regulate the expression of surface antigens to evade the detection by host
immune surveillance. It is thought that PfSir2A achieves this by deacetylating
histones. However, the deacetylase activity of PfSir2A is weak. Here we present
enzymology and structural evidence supporting that PfSir2A catalyzes the
hydrolysis of medium and long chain fatty acyl groups from lysine residues more
efficiently. Furthermore, P. falciparum proteins are found to contain such fatty
acyl lysine modifications that can be removed by purified PfSir2A in vitro.
Together, the data suggest that the physiological function of PfSir2A in antigen
variation may be achieved by removing medium and long chain fatty acyl groups
from protein lysine residues. The robust activity of PfSir2A would also
facilitate the development of PfSir2A inhibitors, which may have therapeutic
value in malaria treatment.
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