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Figure 5.
Fig. 5. Stereofigure of local environment ofFAD in AvFPR showing residues 1-54of the RxYS/T motif, Phe37, residues
252-258, which include a unique C-terminal extension, Cys219 residues 121 of the GT/SGxxP motif. Tyr53 and Phe255 are
involved in stacking interactions with the isoalloxazine and adenine rings of respectively. Ala254 is an aromatic residue in the
EcFldR and enzymes. Water molecules (crosses) occupy the NADPH binding site adjacent to the flavin. The conserved residues
Ser54 Cys219 lie on either side of this cavity. Possible hydrogen bonds are indicated with distances in A. Each phosphate ofFAD
interacts with a basic residue and the carbonyl oxygen of Ala254 is adjacent o N10 of the flavin. Not are the residues f the
helix a1 whose N-terminal dipole is oriented toward the phosphates, and specific hydrogen bonds between 02 and N3 of flavin
and residues on strand 05.
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