Summary for 1CNQ
| Entry DOI | 10.2210/pdb1cnq/pdb |
| Descriptor | FRUCTOSE-1,6-BISPHOSPHATASE, 6-O-phosphono-beta-D-fructofuranose, ZINC ION, ... (5 entities in total) |
| Functional Keywords | bisphosphatase, hydrolase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 37502.68 |
| Authors | Choe, J.,Poland, B.W.,Fromm, H.,Honzatko, R. (deposition date: 1999-05-21, release date: 1999-05-28, Last modification date: 2024-05-22) |
| Primary citation | Choe, J.Y.,Poland, B.W.,Fromm, H.J.,Honzatko, R.B. Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase. Biochemistry, 37:11441-11450, 1998 Cited by PubMed Abstract: A disordered loop (loop 52-72, residues 52-72) in crystal structures of fructose-1,6-bisphosphatase (FBPase) has been implicated in regulatory and catalytic phenomena by studies in directed mutation. A crystal structure of FBPase in a complex with three zinc cations and the products fructose 6-phosphate (F6P) and phosphate (Pi) reveals loop 52-72 for the first time in a well-defined conformation with strong electron density. Loop 52-57 interacts primarily with the active site of its own subunit. Asp68 of the loop hydrogen bonds with Arg276 and a zinc cation located at the putative potassium activation site. Leu56 and Tyr57 of the loop pack against hydrophobic residues from two separate subunits of FBPase. A mechanism of allosteric regulation of catalysis is presented, in which AMP, by binding to its allosteric pocket, displaces loop 52-72 from the active site. Furthermore, the current structure suggests that both the alpha- and beta-anomers of F6P can be substrates in the reverse reaction catalyzed by FBPase. Mechanisms of catalysis are proposed for the reverse reaction in which Asp121 serves as a catalytic base for the alpha-anomer and Glu280 serves as a catalytic base for the beta-anomer. PubMed: 9708979DOI: 10.1021/bi981112u PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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