2f3o

From Proteopedia

Revision as of 17:26, 29 January 2008

Crystal Structure of a glycyl radical enzyme from Archaeoglobus fulgidus

Overview

We have solved the crystal structure of a PFL2 from Archaeglobus fulgidus, at 2.9 A resolution. Of the three previously solved enzyme structures of, glycyl radical enzymes, pyruvate formate lyase (PFL), anaerobic, ribonucleotide reductase and glycerol dehydratase (GD), the last one is, clearly most similar to PFL2. We observed electron density in the active, site of PFL2, which we modelled as glycerol. The orientation of the, glycerol is different from that in GD, and changes in the active site, indicate that the actual substrate of PFL2 is bigger than a glycerol, molecule, but sequence and structural homology suggest that PFL2 may be a, dehydratase. Crystal packing, solution X-ray scattering and, ultracentrifugation experiments show that PFL2 is tetrameric, unlike other, glycyl radical enzymes. A.fulgidus is a hyperthermophile and PFL2 appears, to be stabilized by several factors including an increased number of ion, pairs, differences in buried charges, a truncated N terminus, anchoring of, loops and N terminus via salt-bridges, changes in the oligomeric interface, and perhaps also the higher oligomerization state of the protein.

About this Structure

2F3O is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a glycyl radical enzyme from Archaeoglobus fulgidus., Lehtio L, Grossmann JG, Kokona B, Fairman R, Goldman A, J Mol Biol. 2006 Mar 17;357(1):221-35. Epub 2006 Jan 3. PMID:16414072

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