3CB8

4Fe-4S-Pyruvate formate-lyase activating enzyme in complex with AdoMet and a peptide substrate

Summary for 3CB8

• Entry DOI: 10.2210/pdb3cb8/pdb
• Related: 3C8F
• Descriptor: Pyruvate formate-lyase 1-activating enzyme, peptide substrate VSGYAV, SODIUM ION, ... (7 entities in total)
• Functional Keywords: adomet radical, sam radical, activase, glycyl radical, partial tim barrel, 4fe-4s, carbohydrate metabolism, cytoplasm, glucose metabolism, iron, iron-sulfur, metal-binding, oxidoreductase, s-adenosyl-l-methionine
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A9N4
• Total number of polymer chains: 2
• Total formula weight: 29666.99

Authors

Vey, J.L.,Drennan, C.L. (deposition date: 2008-02-21, release date: 2008-10-28, Last modification date: 2024-02-21)

Primary citation

Vey, J.L.,Yang, J.,Li, M.,Broderick, W.E.,Broderick, J.B.,Drennan, C.L.
Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme.
Proc.Natl.Acad.Sci.Usa, 105:16137-16141, 2008

PubMed Abstract: Pyruvate formate-lyase activating enzyme generates a stable and catalytically essential glycyl radical on G(734) of pyruvate formate-lyase via the direct, stereospecific abstraction of a hydrogen atom from pyruvate formate-lyase. The activase performs this remarkable feat by using an iron-sulfur cluster and S-adenosylmethionine (AdoMet), thus placing it among the AdoMet radical superfamily of enzymes. We report here structures of the substrate-free and substrate-bound forms of pyruvate formate-lyase-activating enzyme, the first structures of an AdoMet radical activase. To obtain the substrate-bound structure, we have used a peptide substrate, the 7-mer RVSGYAV, which contains the sequence surrounding G(734). Our structures provide fundamental insights into the interactions between the activase and the G(734) loop of pyruvate formate-lyase and provide a structural basis for direct and stereospecific H atom abstraction from the buried G(734) of pyruvate formate-lyase.

PubMed: 18852451
DOI: 10.1073/pnas.0806640105

Experimental method

X-RAY DIFFRACTION (2.77 Å)