view article
Figure 7
FtFBPaseII metal sites as found in chain A of the FtFBPaseII tetramer. The right (M4) site has a more conventional octahedral coordination by water molecules plus the side chain of Asp84 (chain A) and the carbonyl group of Leu86 (chain A). On the left is the M1 site created by the extension of Asp116 in FtFBPaseII relative to MtFBPaseII prior to Tyr118. At the bottom, the side chain of Glu328 from the symmetrically related molecule (chain D; purple) bridges the two metal sites. In this structure, the M1 site appears to be unique to this group of class II FBPases and probably corresponds to an Mg2+-inhibited form of the enzyme. FtFBPaseII uses Mn2+ as a metal cofactor for activity.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 76| Part 11| November 2020| Pages 524-535
https://doi.org/10.1107/S2053230X20013370
Follow Acta Cryst. F
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS