9DQ7
Borrelia burgdorferi LDH with NADH, oxamate and FBS
Summary for 9DQ7
| Entry DOI | 10.2210/pdb9dq7/pdb |
| Descriptor | L-lactate dehydrogenase, [[(2~{R},3~{S},4~{R},5~{R})-5-(5-aminocarbonyl-2~{H}-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate, OXAMIC ACID, ... (6 entities in total) |
| Functional Keywords | lactate dehydrogenase, fbs, oxamate, nadh, oxidoreductase |
| Biological source | Borreliella burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 4 |
| Total formula weight | 142213.92 |
| Authors | Lynch, M.J. (deposition date: 2024-09-23, release date: 2025-03-12, Last modification date: 2025-09-24) |
| Primary citation | Sze, C.W.,Lynch, M.J.,Zhang, K.,Neau, D.B.,Ealick, S.E.,Crane, B.R.,Li, C. Lactate dehydrogenase is the Achilles' heel of Lyme disease bacterium Borreliella burgdorferi. Mbio, 16:e0372824-e0372824, 2025 Cited by PubMed Abstract: As a zoonotic pathogen, the Lyme disease bacterium has evolved unique metabolic pathways, some of which are specific and essential for its survival and thus present as ideal targets for developing new therapeutics. dispenses with the use of thiamin as a cofactor and relies on lactate dehydrogenase (BbLDH) to convert pyruvate to lactate for balancing NADH/NAD ratios. This report first demonstrates that BbLDH is a canonical LDH with some unique biochemical and structural features. A loss-of-function study then reveals that BbLDH is essential for survival and infectivity, highlighting its therapeutic potential. Drug screening identifies four previously unknown LDH inhibitors with minimal cytotoxicity, two of which inhibit growth. This study provides mechanistic insights into the function of BbLDH in the pathophysiology of and lays the groundwork for developing genus-specific metabolic inhibitors against and potentially other tick-borne pathogens as well. PubMed: 40111021DOI: 10.1128/mbio.03728-24 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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