Structure of the month - February 2010

Ilari_October09 fig1a

Figure 1a.  Overall fold of L. infantum TR. One monomer of the dimer is coloured gray. In the other monomer, the FAD binding domain (residues 1-160 and 291-360) is coloured red, the NADPH binding domain (residues 161-290)  blue, the interface domain (361-488) in yellow-orange. The FAD and NADPH cofactors are indicated in stick and Sb(III) is indicated as a green sphere. 

Ilari_October09_ fig1b

Figure 1b.  View of the catalytic site and of Sb(III) binding site in the reduced form of TR from Leishmania infantum. The Sb(III) coordinating residues (Cys52, Cys57, His461’ and Thr335), NADPH and FAD molecules are indicated as sticks.


Iliari_October09_table1.png

Table 1. Crystal parameters, data-collection and refinement statistics. Values in parentheses are for the highest resolution shell.