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

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Figure 6
Schematic representation of the active site of the T84S MtFBPaseII structure. The distances of the atoms (Å) found in the T84S MtFBPaseII structure are consistent with the mechanism proposed for EcFBPaseII. The cleaved phosphate and nucleophilic hydroxyl have been added in blue. A possible water has been added bridging the distance between Ser84 and the added phosphate group. This figure was prepared with ChemDraw.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798318002838

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