Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.11 extracted from

  • Gao, Y.; Iancu, C.V.; Mukind, S.; Choe, J.Y.; Honzatko, R.B.
    Mechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase (2013), Biochemistry, 52, 5206-5216.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
mutation I10D introduces an electrostatic charge that destabilizes the R and T states. Structure and molcular dynamic simulation show that the AMP/Mg2+ and AMP/Zn2+ complexes of mutant I10D are in intermediate quaternary conformations completing 12° of the subunit-pair rotation, but the complex with Zn2+ provides an engaged loop in a near-T quaternary state. The 12° subunit-pair rotation generates close contacts involving the hinges, residues 50-57 and hairpin turns, residues 58-72, of the engaged loops. Additional subunit-pair rotation toward the T state would make such contacts unfavorable Sus scrofa

Protein Variants

Protein Variants Comment Organism
I10D mutation introduces an electrostatic charge that destabilizes the R and T states. Structure and molcular dynamic simulation show that the AMP/Mg2+ and AMP/Zn2+ complexes of mutant I10D are in intermediate quaternary conformations completing 12° of the subunit-pair rotation, but the complex with Zn2+ provides an engaged loop in a near-T quaternary state. The 12° subunit-pair rotation generates close contacts involving the hinges, residues 50-57 and hairpin turns, residues 58-72, of the engaged loops. Additional subunit-pair rotation toward the T state would make such contacts unfavorable Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa P00636 isoform FBP1
-