5k54 | pdb_00005k54

Human muscle fructose-1,6-bisphosphatase E69Q mutant in active R-state

spinqualitylabelsall models 5k54, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k54 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3ifa, 3ifc, 4he0, 4he1, 4he2, 5et5, 5et6, 5et7, 5et8 Gene: FBP2 (HUMAN) Activity: Fructose-bisphosphatase, with EC number 3.1.3.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Human fructose-1,6-bisphosphatase is an allosteric enzyme that is regulated by different ligands. There are only two known isozymes in human tissues: the liver isozyme (the key enzyme of gluconeogenesis), which is regulated by fructose 2,6-bisphosphate, and its muscle counterpart (participating in glycogen synthesis), which is regulated by calcium ions. AMP, which is an allosteric inhibitor of both isozymes, inhibits the muscle isozyme with an I(0.5) that is 35-100 times lower than for the liver isozyme and the reason for this difference remains obscure. In studies aiming at an explanation of the main differences in the regulation of the two isozymes, it has been shown that only one residue, in position 69, regulates the sensitivity towards calcium ions. As a consequence of this finding, an E69Q mutant of the muscle isozyme, which is insensitive to calcium ions while retaining all other kinetic properties resembling the liver isozyme, has been prepared and crystallized. Here, two crystal structures of this mutant enzyme in complex with AMP with and without fructose 6-phosphate (the product of the catalytic reaction) are presented. The AMP binding pattern of the muscle isozyme is quite similar to that of the liver isozyme and the T conformations of the two isozymes are nearly the same. Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.,Zarzycki M, Kolodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1028-34. doi:, 10.1107/S090744491104385X. Epub 2011 Nov 18. PMID:22120740 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA