Abstract
We cloned and expressed in Escherichia coli the Archaeglobus fulgidus gene that encodes pyruvate formate lyase 2 (PFL2). PFL2, despite its homology to the other glycyl radical enzymes, differs from them by exhibiting a completely different oligomerization. The most abundant form of PFL2 when expressed in E.coli is a trimer. The closest homologue of PFL2 with a known structure is E. coli PFL, which is a dimer. Sequence comparisons allowed us to reclassify PFL-like enzymes and the consensus sequences allowed us to propose an activation route for PFL-like glycyl radical enzymes. Surprisingly, most of the conserved residues in PFL-like enzymes appear to be involved in preserving the structure, rather than forming the active site.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / chemistry
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Acetyltransferases / classification
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Acetyltransferases / genetics*
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Amino Acid Sequence
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Archaeoglobus fulgidus / enzymology*
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Archaeoglobus fulgidus / genetics
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Catalytic Domain / genetics
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Chromatography, Gel
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Cloning, Molecular
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Consensus Sequence / genetics
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Conserved Sequence / genetics
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Cysteine / genetics
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DNA, Archaeal / chemistry
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DNA, Archaeal / genetics
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Electrophoresis, Polyacrylamide Gel
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Enzyme Activation
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Escherichia coli / genetics
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Light
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Phylogeny
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Protein Structure, Tertiary
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Protein Subunits / chemistry
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Protein Subunits / genetics
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Scattering, Radiation
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
Substances
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DNA, Archaeal
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Protein Subunits
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Recombinant Proteins
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Acetyltransferases
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formate C-acetyltransferase
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Cysteine