ArticleThe Journal of biological chemistry2016
Crystal Structure and Function of PqqF Protein in the Pyrroloquinoline Quinone Biosynthetic Pathway.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 34 citations in OpenAlex.
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- Chromosomal barcodes for simultaneous tracking of near-isogenic bacterial strains in plant microbiota.Nature microbiology · 2024Article
- Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023Review
- Multicopy expression of sigma factor RpoH reduces prodigiosin biosynthesis in Serratia marcescens FS14.Antonie van Leeuwenhoek · 2023Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Biological pincer complexes.ChemCatChem · 2020Article
- A two-component protease inThe Journal of biological chemistry · 2019Article
- Protease-associated import systems are widespread in Gram-negative bacteria.PLoS genetics · 2019Article
- Occurrence, function, and biosynthesis of mycofactocin.Applied microbiology and biotechnology · 2019Review
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6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pyrroloquinoline quinone (PQQ) has received considerable attention due to its numerous important physiological functions. PqqA is a precursor peptide of PQQ with two conserved residues: glutamate and tyrosine. After linkage of the Cγ of glutamate and Cϵ of tyrosine by PqqE, these two residues are hypothesized to be cleaved from PqqA by PqqF. The linked glutamate and tyrosine residues are then used to synthesize PQQ. Here, we demonstrated that the pqqF gene is essential for PQQ biosynthesis as deletion of it eliminated the inhibition of prodigiosin production by glucose. We further determined the crystal structure of PqqF, which has a closed clamshell-like shape. The PqqF consists of two halves composed of an N- and a C-terminal lobe. The PqqF-N and PqqF-C lobes form a chamber with the volume of the cavity of ∼9400 Å(3) The PqqF structure conforms to the general structure of inverzincins. Compared with the most thoroughly characterized inverzincin insulin-degrading enzyme, the size of PqqF chamber is markedly smaller, which may define the specificity for its substrate PqqA. Furthermore, the 14-amino acid-residue-long tag formed by the N-terminal tag from expression vector precisely protrudes into the counterpart active site; this N-terminal tag occupies the active site and stabilizes the closed, inactive conformation. His-48, His-52, Glu-129 and His-14 from the N-terminal tag coordinate with the zinc ion. Glu-51 acts as a base catalyst. The observed histidine residue-mediated inhibition may be applicable for the design of a peptide for the inhibition of M16 metalloproteases.
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