Structures of the Mycobacterium tuberculosis GlpX protein (class II fructose-1,6-bisphosphatase): implications for the active oligomeric state, catalytic mechanism and citrate inhibition

Wolf, N.M.; Gutka, H.J.; Movahedzadeh, F.; Abad-Zapatero, C.

doi:10.1107/S2059798318002838

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 5
Allosteric pocket of FPBaseII. Synechocystis FBP/SBPase (orange) has an allosteric site with AMP bound. T84S MtFBPaseII (light purple) in complex with F6P has malonate bound in the same pocket, but the amino-acid residues are not exclusively conserved. Critically, Tyr279 of MtFBPaseII blocks the AMP-binding site present in Synechocystis FBP/SBPase (PDB entry 3rpl), which contains a phenylalanine residue (Phe309) that interacts with the adenine heterocycle by ring stacking.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 74| Part 4| April 2018| Pages 321-331

https://doi.org/10.1107/S2059798318002838

Open

access

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page