3opy | pdb_00003opy
Crystal structure of Pichia pastoris phosphofructokinase in the T-state
Structural highlights
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Function[PFKA1_PICPA] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184][1] [PFKA3_PICPA] Structural subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Not required for catalytic activity. Fine-tunes allosteric regulation of the ATP-PFK by ATP, fructose 2,6-bisphosphate and AMP.[2] [PFKA2_PICPA] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03184][3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEukaryotic ATP-dependent 6-phosphofructokinases (Pfks) differ from their bacterial counterparts in a much more complex structural organization and allosteric regulation. Pichia pastoris Pfk (PpPfk) is, with approximately 1 MDa, the most complex and probably largest eukaryotic Pfk. We have determined the crystal structure of full-length PpPfk to 3.05 A resolution in the T state. PpPfk forms a (alphabetagamma)4 dodecamer of D2 symmetry with dimensions of 161 x 157 x 233 A mainly via interactions of the alpha chains. The N-terminal domains of the alpha and beta chains have folds that are distantly related to glyoxalase I, but the active sites are no longer functional. Interestingly, these domains located at the 2 distal ends of this protein along the long 2-fold axis form a (alphabeta)2 dimer as does the core Pfk domains; however, the domains are swapped across the tetramerization interface. In PpPfk, the unique gamma subunit participates in oligomerization of the alphabeta chains. This modulator protein was acquired from an ancient S-adenosylmethionine-dependent methyltransferase. The identification of novel ATP binding sites, which do not correspond to the bacterial catalytic or effector binding sites, point to marked structural and functional differences between bacterial and eukaryotic Pfks.-Strater, N., Marek, S., Kuettner, E. B., Kloos, M., Keim, A., Bruser, A., Kirchberger, J., Schoneberg, T. Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases. Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases.,Strater N, Marek S, Kuettner EB, Kloos M, Keim A, Bruser A, Kirchberger J, Schoneberg T FASEB J. 2010 Sep 10. PMID:20833871[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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