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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Proteins. 2011 Apr 12;79(6):1820–1829. doi: 10.1002/prot.23006

FIGURE 2.

FIGURE 2

A Malonate binds to the active-site of PepcA via interactions with His11, Arg82, Ser201 and Gln270. Several strands of the β-barrel are visible in the lower right of the figure. The C-terminal Gly537 positions Arg246, which in turn positions Ser201 and Gln270 (visible under His11) in the active-site.

B An inhibitory PEP analog binds to the active-site of the E. coli Pepc via interactions with Arg396, Arg699, Arg713 and a Mn++ ion (shown in purple). In this view into the active-site, the carboxylate of the inhibitor is directly below the Mn++ ion. His138 and Arg587 (corresponding to C. perfringens His11 and Arg246) are missing from the active-site in this T-state structure.