DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ hasemann-1996-1 The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Hasemann CA., Istvan ES., Uyeda K., Deisenhofer J. hasemann@howie.swmed.edu Structure (0969-2126) 1996 IMEx Only protein-protein interactions imex curation f264_rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 Pfkfb4 6PF-2-K/Fru-2,6-P2ase testis-type isozyme protein protein rat Rattus norvegicus (Rat) Rat MASPRELTQNPLKKIWMPYSNGRPALHASQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDMVKTYKSFEFFLPDNEEGLKIRKQCALAALNDVRKFLSEEGGHVAVFDATNTTRERRAMIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEEQDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFSKHLAQFISDQNIKDLKVWTSQMKRTIQTAEALSVPYEQWKVLNEIDAGVCEEMTYEEIQDHYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEELPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPSEEALVTVPAHQ pfkfb4-1 Homodimerization of 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 demonstrated by x-ray crystallography 252324 N/A 252325 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false working 18.3%, free 25.0% 2.00� Monomers associate in a head-to-head fashion with the 6-phosphofructo-2-kinase domain making contact. Sequence has all trytophans mutated to phenylalanine. Also His256Ala results in enzyme being catalytically inactive. Structure also shows position of ATPgammaS and inorganic phosphate in the molecule