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Table 3 Dimeric and tetrameric contacts in TrmI proteins.

From: Structural comparison of tRNA m1A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions

  A/B dimer A/C dimer Tetrameric assembly
structures N° of interfacing residues in both partners Interface area (Å 2 ) Buried surface area (Å 2 ) N HB 1 N SB 2 N vdW 3 hydrophobic P -value 4 N° of interfacing residues in both partners Interface area (Å 2 ) Buried surface area (Å 2 ) N HB 1 N SB 2 N vdW 3 hydrophobic P -value 4 Buried surface area (Å 2) ΔGint 5 kcal/mol ΔGdiss 6 kcal/mol
M. tuberculosis 76+75 2378.4 4760 28 6 (0) 30 0.299 23+23 788.7 1580 10 4 (2) 10 0.22 13160 -69.5 24.7
T. thermophilus 95+62 2478.1 4960 21 18 (5) 30 0.776 22+22 731.3 1460 12 4 (2) 13 0.423 13390 -25.9 20.8
T. maritima 87+87 3150.2 6160 24 36 (4) 103 0.356 24+24 879.5 1810 10 4 (2) 22 0.668 16750 -47.9 3.0
A. aeolicus 65+65 2596.3 5200 34 14 (0) 44 0.059 22+24 856.5 1710 12 4 (2) 4 0.416 14410 -54.7 15.1
P. abyssi 65+65 2311.5 4620 17 14 (6) 30 0.006 24+24 775.6 1550 12 0 10 0.069 12840 -86.6 41.0
  1. 1Number of H-bonds less than 3.2 Å across the interface (per monomer).
  2. 2Number of salt bridges less than 3.6 Å across the interface (per monomer). The number of bidentate ionic interactions is indicated in parentheses.
  3. 3Number of van der Waals interactions less than 4.2 Å (per monomer)
  4. 4defined as the probability to find a same-area patch on protein surface that would be more hydrophobic than the interface
  5. 5solvation free energy gain upon formation of the assembly
  6. 6free energy difference between dissociated and associated states