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PDBsum entry 3wv7
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References listed in PDB file
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Key reference
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Title
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Protein-Pyridinol thioester precursor for biosynthesis of the organometallic acyl-Iron ligand in [fe]-Hydrogenase cofactor.
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Authors
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T.Fujishiro,
J.Kahnt,
U.Ermler,
S.Shima.
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Ref.
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Nat Commun, 2015,
6,
6895.
[DOI no: ]
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PubMed id
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Abstract
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The iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase contains a
prominent iron centre with an acyl-Fe bond and is the only acyl-organometallic
iron compound found in nature. Here, we identify the functions of HcgE and HcgF,
involved in the biosynthesis of the FeGP cofactor using structure-to-function
strategy. Analysis of the HcgE and HcgF crystal structures with and without
bound substrates suggest that HcgE catalyses the adenylylation of the carboxy
group of guanylylpyridinol (GP) to afford AMP-GP, and subsequently HcgF
catalyses the transesterification of AMP-GP to afford a Cys (HcgF)-S-GP
thioester. Both enzymatic reactions are confirmed by in vitro assays. The
structural data also offer plausible catalytic mechanisms. This strategy of
thioester activation corresponds to that used for ubiquitin activation, a key
event in the regulation of multiple cellular processes. It further implicates a
nucleophilic attack onto the acyl carbon presumably via an electron-rich Fe(0)-
or Fe(I)-carbonyl complex in the Fe-acyl formation.
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