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PDBsum entry 6h0c
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Oxidoreductase
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PDB id
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6h0c
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DOI no:
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J Struct Biol
205:91
(2019)
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PubMed id:
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Analysis of a new flavodiiron core structural arrangement in Flv1-ΔFlR protein from Synechocystis sp. PCC6803.
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P.T.Borges,
C.V.Romão,
L.M.Saraiva,
V.L.Gonçalves,
M.A.Carrondo,
M.Teixeira,
C.Frazão.
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ABSTRACT
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Flavodiiron proteins (FDPs) play key roles in biological response mechanisms
against oxygen and/or nitric oxide; in particular they are present in oxygenic
phototrophs (including cyanobacteria and gymnosperms). Two conserved domains
define the core of this family of proteins: a N-terminal
metallo-β-lactamase-like domain followed by a C-terminal flavodoxin-like one,
containing the catalytic diiron centre and a FMN cofactor, respectively. Members
of the FDP family may present extra modules in the C-terminus, and were
classified into several classes according to their distribution and composition.
The cyanobacterium Synechocystis sp. PCC6803 contains four Class C FDPs (Flv1-4)
that include at the C-terminus an additional NAD(P)H:flavin oxidoreductase (FlR)
domain. Two of them (Flv3 and Flv4) have the canonical diiron ligands (Class C,
Type 1), while the other two (Flv1 and Flv2) present different residues in that
region (Class C, Type 2). Most phototrophs, either Bacterial or Eukaryal,
contain at least two FDP genes, each encoding for one of those two types.
Crystals of the Flv1 two core domains (Flv1-ΔFlR), without the C-terminal
NAD(P)H:flavin oxidoreductase extension, were obtained and the structure was
determined. Its pseudo diiron site contains non-canonical basic and neutral
residues, and showed anion moieties, instead. The presented structure revealed
for the first time the structure of the two-domain core of a Class C-Type 2 FDP.
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');
}
}
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