Table II.
Loss of function mutations in A. thaliana ILL2 homologs.
| Mutation | Corresponding residue in ILL2 | Is highly conserved residue? | Distance between Cα and metal 1 [Å] | Structural hypothesis about of origins of the defect |
|---|---|---|---|---|
| E69Ka | E68 | yes | 15.0 | Conformation of the loop harboring general base Glu172 and metal ligand Glu173 will be altered due to loss of stabilizing hydrogen-bond. Possible salt bridge to Asp114 could further disturb local geometry next to the active site. |
| G139Da | G138 | yes | 8.0 | Steric clash resulting from the mutation will directly compromise positioning of metal coordinating residues Cys137 and His139. |
| G415Ea | G411 | no | 18.2 | Mutation places bulky, charged residue into a hydrophobic core of the protein formed by Met145, Ile196, Leu198, Leu384, Val407, and Ile414. Protein likely misfolds. |
| S206Lb | S209 | no | 18.5 | Mutation results in a loss of hydrogen bonds to His380 and fully conserved Asn337. Bulkier, hydrophobic residue at this position may disturbs Phe381 which is involved in formation of, the indole-binding hydrophobic pocket. |
| G224Eb | G227 | yes | 41.6 | Not clear. Residue is located at the tip of the satellite domain. |
| G226Eb | G229 | no | Not clear, residue not resolved in the structure of ILL2. Residue is likely located at the tip of the satellite domain. | |
| A230Tb | A233 | no | Not clear, residue not resolved in the structure of ILL2. Residue is likely located at the tip of the satellite domain. |