 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](wd5166fig2mag.jpg)
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Figure 2
Sequence alignment of Y. pestis RipC with other citrate lyase β subunits (M. tuberculosis CitE, PDB entry 1u5h ; D. radiodurans, PDB entry 1sgj ; B. xenovorans, PDB entry 3r4i ; R. eutropha, PDB entry 3qqw ), as well as H. volcanii malate synthase H (PDB entry 3oyz ; Bracken et al., 2011  ). Cylinders and arrows define the regions of α-helices and β-strands, respectively. Dotted secondary-structure elements are predicted by JPred (Cole et al., 2008) and represent regions missing in the RipC crystal structure. RipC residues that are proposed to interact with CoA or a CoA derivative, based on sequence conservation with H. volcanii malate synthase H, are indicated by asterisks; fully conserved residues are boxed. |
![[Figure 2]](wd5166fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
