3SK3

Crystal structure of Salmonella typhimurium acetate kinase (AckA) with citrate bound at the dimeric interface

Summary for 3SK3

• Entry DOI: 10.2210/pdb3sk3/pdb
• Related: 1G99 1SAZ 2E1Y 2IIR 3KHY 3P4I
• Descriptor: Acetate kinase, CITRIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: actin-like atpase domain, askha superfamily of phosphotransferase, acetokinase, atp binding, phosphotransferase, transferase
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Cellular location: Cytoplasm (By similarity): P63411
• Total number of polymer chains: 2
• Total formula weight: 90552.88

Authors

Chittori, S.,Savithri, H.S.,Murthy, M.R.N. (deposition date: 2011-06-22, release date: 2012-08-29, Last modification date: 2024-10-30)

Primary citation

Chittori, S.,Savithri, H.S.,Murthy, M.R.N.
Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface
Bmc Struct.Biol., 12:24-24, 2012

PubMed Abstract: Bacteria such as Escherichia coli and Salmonella typhimurium can utilize acetate as the sole source of carbon and energy. Acetate kinase (AckA) and phosphotransacetylase (Pta), key enzymes of acetate utilization pathway, regulate flux of metabolites in glycolysis, gluconeogenesis, TCA cycle, glyoxylate bypass and fatty acid metabolism.

PubMed: 23031654
DOI: 10.1186/1472-6807-12-24

Experimental method

X-RAY DIFFRACTION (1.9 Å)