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PEDS Advance Access published online on August 3, 2004
Protein Engineering Design and Selection, doi:10.1093/protein/gzh059
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Received July 12, 2004
Accepted July 13, 2004

Article

The pyruvate formate lyase family: sequences, structures and activation

Lehtiö L. 1 Goldman A. 1*

1 Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, PO Box 65, FIN-00014, Helsinki, Finland

* To whom correspondence should be addressed. E-mail: adrian.goldman{at}helsinki.fi.


  Abstract

We cloned and expressed in E. 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.

Keywords: pyruvate formate lyase; radical; activation; trimer.
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