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![[Figure 2]](ag5063fig2mag.jpg)
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Figure 2
(a) Close-up view of the putative TANGO2 active site. The N-terminal Cys2 and three residues, Asp27, Asn157 and Lys166, are shown in stick representation. Superposition of conserved active-site residues in four known cysteine Ntn-hydrolases and TANGO2 with side chains colored tan (TANGO2, PDB entry 8sv7), blue (PDB entry 2x1d), plum (PDB entry 2hf0), coral (PDB entry 5u7z) and green (PDB entry 6dxx), respectively. Only TANGO2 residue numbers are shown for clarity. Lys166 in TANGO2 is replaced by arginine in all four cysteine Ntn-hydrolases. (b) The water-mediated hydrogen-bonding network of the putative TANGO2 active site. Hydrogen bonds are shown as blue dashed lines. (c) The sulfate ion (  ) binding site of TANGO2. The anion is approximately 10.76 Å from the N-terminal Cys2 and coordinated by a triad of positively charged residues: Arg32, Lys56 and Arg88. (d) The conserved surface phenylalanine in TANGO2 and cysteine Ntn-hydrolases. Structural alignment shows that the surface-exposed Phe29 in TANGO2 is conserved across all four cysteine Ntn-hydrolases (Phe23 of PDB entry 2hf0, Phe123 of PDB entry 2x1d, Phe163 of PDB entry 5u7z and Phe148 of PDB entry 6dxx). |
![[Figure 2]](ag5063fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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