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![[Figure 3]](jb5034fig3mag.jpg)
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Figure 3
Comparison of HsADA1 with other structures of mammalian ADA1 enzymes. (a) Overlay of holo HsADA1 monomer A (magenta) with the unpublished structure of substrate/Ni2+-bound HsADA1 (PDB entry 3iar, lime green). (b) Comparison of Zn2+ and Ni2+ coordination in HsADA1 and PDB entry 3iar, respectively. (c) Enlarged view of the C-terminal helix (residues 354–364) that is present in PDB entry 3iar but absent in HsADA1. (d) Overlay of holo HsADA1 monomer A (magenta) and holo BtADA (cyan) with enlarged views of the Zn2+ environment, C-terminal helix and structural gate. HsADA1 adopts an open conformation with shifts in Leu58, Leu62 and the Leu182–Asp185 loop compared with the closed conformation of holo BtADA. (e) Comparison of the structural gate of HsADA1 monomer A (magenta) with MmADA complexed with DCF (brown) and 1-deaza-adenosine (light blue) and with BtADA complexed with EHNA (orange) and FR235380 (lime green). HsADA1 has similar structural features at the catalytic gate to the closed conformation adopted by MmADA–inhibitor complexes, while displaying shifts in this region from the open conformation adopted by BtADA–inhibitor complexes. (f) Overlay of monomer A (magenta) with holo MmADA (yellow) with enlarged views of the Zn2+ environment, C-terminal site and structural gate. The structural features of the catalytic gate of HsADA1 overlap closely with those of holo MmADA. |
![[Figure 3]](jb5034fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
