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PEDS Advance Access originally published online on August 3, 2004
Protein Engineering Design and Selection 2004 17(6):545-552; doi:10.1093/protein/gzh059
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Protein Engineering, Design & Selection vol. 17 no. 6 © Oxford University Press 2004; all rights reserved

The pyruvate formate lyase family: sequences, structures and activation

L. Lehtiö1,2 and A. Goldman2,3

1Graduate School in Informational and Structural Biology and 2Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, PO Box 65, FIN-00014 Helsinki, Finland

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

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.

Received July 12, 2004; accepted July 13, 2004.

Edited by Joel Sussman


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