Structural highlights
5huq is a 2 chain structure with sequence from "lactobacillus_arabinosus"_fred_et_al. "lactobacillus arabinosus" fred et al.. This structure supersedes the now removed PDB entry 4yns. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Gene: | AB662_09960, ADS73_14595, AKJ11_11795, AN634_09100, AOZ08_01600, IV39_GL000121, JM48_0086, Nizo2877_0389, WU67_00115 ("Lactobacillus arabinosus" Fred et al.) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
METALLOPROTEINS. A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase.,Desguin B, Zhang T, Soumillion P, Hols P, Hu J, Hausinger RP Science. 2015 Jul 3;349(6243):66-9. doi: 10.1126/science.aab2272. PMID:26138974[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Desguin B, Zhang T, Soumillion P, Hols P, Hu J, Hausinger RP. METALLOPROTEINS. A tethered niacin-derived pincer complex with a nickel-carbon bond in lactate racemase. Science. 2015 Jul 3;349(6243):66-9. doi: 10.1126/science.aab2272. PMID:26138974 doi:http://dx.doi.org/10.1126/science.aab2272
