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Figure 3
Structural overlay of Y. pestis RipC (blue), B. xenovorans citrate lyase β subunit (green) and H. volcanii malate synthase H (MSH, red), in which the TIM barrels superimpose upon one another and are shown in ribbon representation. The C-terminal domains from B. xenovorans and H. volcanii are shown in cartoon representation. The dotted line connecting the TIM barrel to the C-terminal domain in MSH suggests a possible intramonomer interaction, although an intermonomer interaction between the C-terminal domain and an adjacent TIM barrel cannot be ruled out. Expanded region: stick representation of active-site residues that are conserved between RipC (blue) and MSH (red). Additional corresponding conserved residues from MSH that are missing from the RipC structure are depicted in parentheses. Acetyl-CoA and pyruvate from MSH are represented as stick models, with C atoms in green, N atoms in blue, O atoms in red, S atoms in yellow and P atoms in orange.

ISSN: 2053-230X
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