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PDBsum entry 5gxv
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Protein transport
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PDB id
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5gxv
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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 mbp-Pigg fusion protein and the essential function of pigg in the prodigiosin biosynthetic pathway in serratia marcescens fs14.
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Authors
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F.Zhang,
Q.Wei,
H.Tong,
D.Xu,
W.Wang,
T.Ran.
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Ref.
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Int J Biol Macromol, 2017,
99,
394-400.
[DOI no: ]
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PubMed id
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Abstract
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Prodigiosin, a tripyrrole red pigment is synthesized by Serratia and some other
microbes through a bifurcated biosynthesis pathway; MBC
(4-methoxy-2,2'-bipyrrole-5-carbaldehyde) and MAP (2-methyl-3-n-amyl-pyrrole)
are synthesized separately and then condensed by PigC to form prodigiosin. PigI,
PigG and PigA have been shown to be involved in the first steps of MBC
biosynthesis (proline incorporation). The crystal structure of PigG was resolved
to elucidate its function and mechanism. PigG, an acyl carrier protein (ACP),
features the ACP architecture:, a helical bundle fold containing three major
helices and a minor distorted helix together with a conserved "S"
motif. An in-frame deletion mutation of the pigG gene abolished the synthesis of
prodigiosin in Serratia marcescens FS14. The production of prodigiosin was fully
restored by complementation of intact pigG; however the S36A mutant was not able
to restore function in the in-frame deletion pigG mutant, indicating that PigG
and the conserved serine residue (S36) of PigG are essential for the synthesis
of prodigiosin.
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