 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](tt5030fig3mag.jpg)
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Figure 3
Structure-driven sequence alignment of OTCases from C. jejuni (Cje aOTC), human (Hum aOTC), P. furiosus (Pfu aOTC), M. tuberculosis (Mtu aOTC), E. coli (Eco aOTC), L. hilgardii (Lhi cOTC) and P. aeruginosa (Pae cOTC). Residue numbering and secondary-structure elements are presented for Cje aOTC. β-Strands are shown as arrows; α-helices and 310-helices are shown as red and blue coils, respectively. Residues that are proposed to be involved in substrate binding are marked with an orange circle. Conserved residues are highlighted in bold. Residues that form the interface between OTC trimers in the respective hexamer, pseudohexamer or dodecamer are marked in blue. The intensity of the color corresponds to the percentage of chains in the oligomeric assembly in which the residue participates in the interface between trimers. Eco aOTC and Hum aOTC do not form this type of oligomeric assembly; therefore, they were not analysed. |
![[Figure 3]](tt5030fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
