Table 3 Comparison of dimer contacts in structurally characterized HU proteins with known thermal stability.

From: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3

 

Source organism*

Buried surface area of a monomer at the interface, Å2 (%)

Total surface area of a monomer, Å2

Hydrogen bonds (shorter than 3.5 Å)

Salt bridges (shorter than 4.0 Å)

Number of residues involved in the interface (hydrophobic) per monomer

ΔiG, kcal/mol

1

Spiroplasma melliferum

2267.0 (30.2)

7508.3

14

0

52 (35)

−44, 3

2

Escherichia coli (HUα2)

1773.3 (32.7)

5419.0

5

6

46 (38)

−35, 2

3

Escherichia coli (HUβ2)

1810.9 (34.2)

5300.3

9

4

47 (30)

−32.2

4

Thermotoga maritima

1868.9 (33.4)

5595.3

7

5

47 (32)

−40.1

5

Bacillus stearothermophilus

1778.4 (27.8)

6404.9

6

4

44 (33)

−41.4

  1. The numbers of hydrogen bonds, salt bridges, and hydrophobic residues at the dimer interface were calculated by WHATIF and manually checked.
  2. *The name of the source organism is underlined if the corresponding HU protein has high thermal stability.
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