Table 3. Analysis of the interface between helix H1 and the C-terminal region of DsbA structures.
The buried surface area (BSA) in helix H1 (column 3) was determined using PISA analysis (Krissinel & Henrick, 2007 ▶). DsbAs, their PDB codes (column 1, in parentheses) and the residue ranges in helix H1 (column 2, in parentheses) and the C-terminal region (column 4, in parentheses) included in the PISA analysis are listed. The percentage of surface area buried in helix H1 relative to its total accessible surface area (∼2000 Å2) is given in column 3 (in parentheses). For MtbDsbA and EcDsbA, BSA and the values reported for the percentage of surface area buried are an average of two MtbDsbA chains (molecule 1 and molecule 2 in the asymmetric unit) and nine EcDsbA chains [PDB entries 1dsb (two chains; Martin et al., 1993 ▶), 1fvk (two chains; Guddat et al., 1997 ▶), 1a2m (two chains; Guddat et al., 1998 ▶), 1a2l (two chains; Guddat et al., 1998 ▶) and 1a2j (one chain; Guddat et al., 1998 ▶)].
| Protein (PDB code) | No. of interfacing residues in helix H1 | Helix H1 BSA (Å2) | No. of interfacing residues in C-terminal region |
|---|---|---|---|
| MtbDsbA | 13 (89–109) | 592 ± 4 (29.6) | 18 (226–255) |
| EcDsbA | 9 (30–50) | 401 ± 42 (18.9) | 10 (168–188) |
| BsDsbA (3eu3; Crow et al., 2009 ▶) | 8 (69–91) | 355 (15.9) | 8 (205–222) |
| SaDsbA (3bci; Heras et al., 2008 ▶) | 9 (26–46) | 370 (15.8) | 7 (167–178) |
| PaDsbA (3h93; Shouldice et al., 2010 ▶) | 7 (37–55) | 282 (14.3) | 9 (166–192) |
| VcDsbA (1bed; Hu et al., 1997 ▶) | 8 (30–48) | 261 (13.7) | 6 (164–181) |
| WpDsbA (3f4r; Kurz et al., 2009 ▶) | 9 (51–71) | 363 (16.5) | 9 (196–218) |
| NmDsbA1 (3a3t; Vivian et al., 2009 ▶) | 7 (57–74) | 290 (15.5) | 7 (189–212) |