5HUQ

A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase

Replaces:  4YNS

Summary for 5HUQ

• Entry DOI: 10.2210/pdb5huq/pdb
• Descriptor: Lactate racemization operon protein LarA, 3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium, SULFATE ION, ... (4 entities in total)
• Functional Keywords: isomerase, racemase, nickel, cofactor
• Biological source: Lactobacillus plantarum
• Total number of polymer chains: 2
• Total formula weight: 97711.88

Authors

Desguin, B.,Zhang, T.,Soumillion, P.,Hols, P.,Hu, J.,Hausinger, R.P. (deposition date: 2016-01-27, release date: 2016-02-10, Last modification date: 2024-11-13)

Primary citation

Desguin, B.,Zhang, T.,Soumillion, P.,Hols, P.,Hu, J.,Hausinger, R.P.
METALLOPROTEINS. A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase.
Science, 349:66-69, 2015

PubMed Abstract: Lactic acid racemization is involved in lactate metabolism and cell wall assembly of many microorganisms. Lactate racemase (Lar) requires nickel, but the nickel-binding site and the role of three accessory proteins required for its activation remain enigmatic. We combined mass spectrometry and x-ray crystallography to show that Lar from Lactobacillus plantarum possesses an organometallic nickel-containing prosthetic group. A nicotinic acid mononucleotide derivative is tethered to Lys(184) and forms a tridentate pincer complex that coordinates nickel through one metal-carbon and two metal-sulfur bonds, with His(200) as another ligand. Although similar complexes have been previously synthesized, there was no prior evidence for the existence of pincer cofactors in enzymes. The wide distribution of the accessory proteins without Lar suggests that it may play a role in other enzymes.

PubMed: 26138974
DOI: 10.1126/science.aab2272

Experimental method

X-RAY DIFFRACTION (3 Å)