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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Desguin, Benoît Zhang, Tuo Hols, Pascal Soumillion, Patrice Hu, Jian Hausinger, Robert P. |
| Description | Author Affiliation: Desguin B ( Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA.); Zhang T ( Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.); Soumillion P ( Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium.); Hols P ( Institute of Life Sciences, Université Catholique de Louvain, B-1348 Louvain-la-Neuve, Belgium.); Hu J ( Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. Department of Chemistry, Michigan State University, East Lansing, MI 48824, USA. hujian1@msu.edu hausinge@msu.edu.); Hausinger RP ( Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. hujian1@msu.edu hausinge@msu.edu.) |
| 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. |
| ISSN | 00368075 |
| Issue Number | 6243 |
| Volume Number | 349 |
| e-ISSN | 10959203 |
| Journal | Science |
| Language | English |
| Publisher | American Association for the Advancement of Science (United States) |
| Publisher Date | 2015-07-03 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Bacterial Proteins Chemistry Lactic Acid Biosynthesis Lactobacillus Plantarum Enzymology Metalloproteins Niacin Nickel Racemases And Epimerases Genetics Binding Sites Carbon Catalysis Crystallography, X-Ray Histidine Holoenzymes Ligands Lysine Nicotinamide Mononucleotide Analogs & Derivatives Protein Processing, Post-Translational Protein Structure, Secondary Spectrometry, Mass, Electrospray Ionization Sulfur Journal Article Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | History and Philosophy of Science |
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