Journal:JMB:2

From Proteopedia

Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1

Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD ^[1]

Molecular Tour

New 2HQ/rePON1 complex at pH 6.5 (active-site loop residues shown in ball-and-stick)
New rePON1 at pH 6.5
Old rePON1 at pH 4.5

Figure   2.   Structural   details   of   the   2HQ/rePON1   complex   at   pH   6.5;   2HQ   and   the   structured  active-­site  loop  in  the  rePON1-­2HQ  complex  structure.    Overlay  of  the  phosphate  ion  in  the  apo  rePON1  at  pH  6.5  and  of  2HQ   in  the  rePON1-­2HQ  complex.   The  first  segment  of  the  active-­site  loop,  and  residues  Y71   and  I74  in  particular,  comprises  part  of  PON1's  active-­site  wall.   Interactions  of  2HQ  with   active-­site  residues  (interactions  with  the  catalytic  Ca2+  are  highlighted  in  red).  

1. ↑ Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS. Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1. J Mol Biol. 2012 Mar 1. PMID:22387469 doi:10.1016/j.jmb.2012.02.042