Figure 3.

Comparative analysis of the N-terminal domains of FAH superfamily members. (A–G) All 21 FAH members available in the Protein Data Bank to date were grouped according to the overall structure of their N-terminal domains. Only one member of each cluster (quite often a dimeric protein) was chosen to represent the overall fold of the group. Representative tertiary and quaternary structures of enzymes from (A) Mus musculus (PDB entry 1QCN ⁽³⁰⁾ and Burkholderia cenocepacia (PDB entry 4QKU); (B) Sulfolobus solfataricus (PDB entry 2Q18 ⁽³²⁾; (C) Mycobacterium marinum (PDB entry 3QDF ⁽³⁹⁾, Thermus thermophilus (PDB entry 2DFU and PDB entry 1WZO), M. abscessos (PDB entry 3RR6 ⁽³⁹⁾, Corynebacterium glutamicum (PDB entry 4DBF ⁽³³⁾, and M. smegmatis (PDB entry 4PFZ); (D) M. abscessos (PDB entry 3R6O ⁽³⁹⁾ and Sinorhizobium meliloti (PDB entry 3LZK); (E) Homo sapiens (PDB entry 1SAW ⁽³¹⁾, E. coli (PDB entry 1NR9), Yersinia pestis (PDB entry 3S52), Oleispira antarctica (PDB entry 3V77 ⁽⁴⁰⁾, B. cenocepacia (PDB entry 4MAQ) and Saccharomyces cerevisiae (PDB entry 1NKQ); (F) E. coli HpcE (PDB entry 1GTT ⁽¹⁰⁾ and (G) E. coli HpcG (PDB entry 2EB4 ⁽¹¹⁾, E. coli MhpD (PDB entry 2WQT ⁽⁹⁾ and P. putida NahK (this work). (H) Superposition of representative monomers showing the conserved CTD (incomplete β-barrel and β-sheet) and the position of each NTD.