EC Number   |
Subunits |
Reference |
|---|
  1.1.1.313 | homotetramer |
4 * 27000, about, sequence calculation |
762706 |
| 1.1.1.313 | homotetramer |
in the tetrameric structure of IsfD, the respective diagonal subunits cross-interact strongly via their C-terminal tails. The latter region with beta-sheets 8 and 9 protrudes away from the main subunit body and reaches the active site of the opposite subunit. Thus, stabilization of the substrate-binding loop in the closed conformation is accomplished. In particular, C-terminal residue F248 is located close to side chains of active site amino acids I142 and Y148 of the diagonal subunit. This important interaction results in a proper positioning of Y148 for hydrogen bonding with the sulfonate group of isethionate. Enzyme structure comparisons, detailed overview |
762708 |
| 1.1.1.313 | More |
IsfD forms a homotetramer in both crystal and solution states, with the C-terminal tail of each subunit interacting with the C-terminal tail of the diagonally opposite subunit, forming an antiparallel beta-sheet that constitutes part of the substrate-binding site. The sulfonate group of isethionate is stabilized by a hydrogen bond network formed by the residues Y148, R195, Q244 and a water molecule. In addition, F249 from the diagonal subunit restrains the conformation of Y148 to further stabilize the orientation of the sulfonate group. Quaternary, subunit structure of IsfD and the structure-based sequence alignments of IsfD with selected SDR members, overview |
762706 |
