5I2G

1,2-propanediol Dehydration in Roseburia inulinivorans; Structural Basis for Substrate and Enantiomer Selectivity

Summary for 5I2G

• Entry DOI: 10.2210/pdb5i2g/pdb
• Related: 5I2A
• Descriptor: Diol dehydratase, S-1,2-PROPANEDIOL (3 entities in total)
• Functional Keywords: diol dehydratase, glycyl radical enzymes, enzyme structure, lyase
• Biological source: Roseburia inulinivorans
• Total number of polymer chains: 2
• Total formula weight: 188381.36

Authors

LaMattina, J.W.,Reitzer, P.,Kapoor, S.,Galzerani, F.,Koch, D.J.,Gouvea, I.E.,Lanzilotta, W.N. (deposition date: 2016-02-08, release date: 2016-06-01, Last modification date: 2024-05-22)

Primary citation

LaMattina, J.W.,Keul, N.D.,Reitzer, P.,Kapoor, S.,Galzerani, F.,Koch, D.J.,Gouvea, I.E.,Lanzilotta, W.N.
1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY.
J.Biol.Chem., 291:15515-15526, 2016

PubMed Abstract: Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical reactions. In this work we present the first biochemical and structural data for a GRE-type diol dehydratase from the organism Roseburia inulinivorans (RiDD). Despite high sequence (48% identity) and structural similarity to the GRE-type glycerol dehydratase from Clostridium butyricum, we demonstrate that the RiDD is in fact a diol dehydratase. In addition, the RiDD will utilize both (S)-1,2-propanediol and (R)-1,2-propanediol as a substrate, with an observed preference for the S enantiomer. Based on the new structural information we developed and successfully tested a hypothesis that explains the functional differences we observe.

PubMed: 27252380
DOI: 10.1074/jbc.M116.721142

Experimental method

X-RAY DIFFRACTION (2.352 Å)