6MNV

Crystal structure of X. citri phosphoglucomutase in complex with CH2FG1P

Summary for 6MNV

• Entry DOI: 10.2210/pdb6mnv/pdb
• Related: 6mlf 6mlh 6mlw
• Descriptor: Phosphomannomutase/phosphoglucomutase, 1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: enzyme, carbohydrate biosynthesis, isomerase
• Biological source: Xanthomonas citri
• Total number of polymer chains: 1
• Total formula weight: 51604.13

Authors

Beamer, L.,Stiers, K. (deposition date: 2018-10-03, release date: 2019-07-31, Last modification date: 2023-10-11)

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

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: 31264865
DOI: 10.1021/acs.joc.9b01305

Experimental method

X-RAY DIFFRACTION (1.65 Å)