2YJG

Structure of the lactate racemase apoprotein from Thermoanaerobacterium thermosaccharolyticum

Summary for 2YJG

• Entry DOI: 10.2210/pdb2yjg/pdb
• Descriptor: LACTATE RACEMASE APOPROTEIN, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: isomerase, nickel-dependent enzyme
• Biological source: THERMOANAEROBACTERIUM THERMOSACCHAROLYTICUM
• Total number of polymer chains: 2
• Total formula weight: 96852.85

Authors

Declercq, J.P.,Desguin, B.,Soumillion, P.,Hols, P. (deposition date: 2011-05-19, release date: 2012-05-30, Last modification date: 2024-05-01)

Primary citation

Desguin, B.,Goffin, P.,Viaene, E.,Kleerebezem, M.,Martin-Diaconescu, V.,Maroney, M.J.,Declercq, J.,Soumillion, P.,Hols, P.
Lactate Racemase is a Nickel-Dependent Enzyme Activated by a Widespread Maturation System.
Nat.Commun., 5:3615-, 2014

PubMed Abstract: Racemases catalyse the inversion of stereochemistry in biological molecules, giving the organism the ability to use both isomers. Among them, lactate racemase remains unexplored due to its intrinsic instability and lack of molecular characterization. Here we determine the genetic basis of lactate racemization in Lactobacillus plantarum. We show that, unexpectedly, the racemase is a nickel-dependent enzyme with a novel α/β fold. In addition, we decipher the process leading to an active enzyme, which involves the activation of the apo-enzyme by a single nickel-containing maturation protein that requires preactivation by two other accessory proteins. Genomic investigations reveal the wide distribution of the lactate racemase system among prokaryotes, showing the high significance of both lactate enantiomers in carbon metabolism. The even broader distribution of the nickel-based maturation system suggests a function beyond activation of the lactate racemase and possibly linked with other undiscovered nickel-dependent enzymes.

PubMed: 24710389
DOI: 10.1038/NCOMMS4615

Experimental method

X-RAY DIFFRACTION (1.8 Å)