6MLH
Crystal structure of X. citri phosphoglucomutase in complex with GLUCOPYRANOSYL-1-METHYL-PHOSPHONIC ACID
Summary for 6MLH
| Entry DOI | 10.2210/pdb6mlh/pdb |
| Descriptor | Phosphoglucomutase, (1S)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | enzyme, carbohydrate biosynthesis, isomerase |
| Biological source | Xanthomonas citri |
| Total number of polymer chains | 1 |
| Total formula weight | 51499.94 |
| Authors | Beamer, L.,Stiers, K. (deposition date: 2018-09-27, release date: 2019-07-31, Last modification date: 2024-11-06) |
| Primary citation | Zhu, J.S.,Stiers, K.M.,Soleimani, E.,Groves, B.R.,Beamer, L.J.,Jakeman, D.L. Inhibitory Evaluation of alpha PMM/PGM fromPseudomonas aeruginosa: Chemical Synthesis, Enzyme Kinetics, and Protein Crystallographic Study. J.Org.Chem., 84:9627-9636, 2019 Cited by PubMed Abstract: α-Phosphomannomutase/phosphoglucomutase (αPMM/PGM) from is involved in bacterial cell wall assembly and is implicated in virulence, yet few studies have addressed αPMM/PGM inhibition from this important Gram-negative bacterial human pathogen. Four structurally different α-d-glucopyranose 1-phosphate (αG1P) derivatives including 1--fluoromethylated analogues (-), 1,2-cyclic phosph(on)ate analogues (-), isosteric methylene phosphono analogues ( and ), and 6-fluoro-αG1P (), were synthesized and assessed as potential time-dependent or reversible αPMM/PGM inhibitors. The resulting kinetic data were consistent with the crystallographic structures of the highly homologous αPGM with inhibitors and - binding to the enzyme active site (1.65-1.9 Å). These structural and kinetic insights will enhance the design of future αPMM/PGM inhibitors. PubMed: 31264865DOI: 10.1021/acs.joc.9b01305 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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