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Literature summary extracted from

  • Soederholm, A.; Guo, X.; Newton, M.S.; Evans, G.B.; Naesvall, J.; Patrick, W.M.; Selmer, M.
    Two-step ligand binding in a (betaalpha)8 barrel enzyme Substrate-bound structures shed new light on the catalytic cycle of HisA (2015), J. Biol. Chem., 290, 24657-24668 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.16
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.16 wild type in its apo-state and mutants D7N and D7N/D176A in complex with two different conformations of the labile substrate N'-[(5'-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide, i.e. ProFAR. Residue D7 acts as the catalytic base, and D176 acts as the catalytic acid Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.16 D7N residue D7 acts as the catalytic base, crystallization data Salmonella enterica subsp. enterica serovar Typhimurium
5.3.1.16 D7N/D176A residue D7 acts as the catalytic base, and D176 acts as the catalytic acid, crystallization data Salmonella enterica subsp. enterica serovar Typhimurium

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.16 Salmonella enterica subsp. enterica serovar Typhimurium P10372
-
-
5.3.1.16 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 P10372
-
-

General Information

EC Number General Information Comment Organism
5.3.1.16 physiological function catalytic mechanism involves long loops on the catayltic face that enclose the substrate. Substrate ProFAR adopts an extended conformation where its non-reacting half is in a product-like conformation. This change is associated with shifts in a hydrogen bond network including residues His47, Asp129, Thr171, and Ser202 Salmonella enterica subsp. enterica serovar Typhimurium