Table 1.
Individual structural characteristics related to activation state in X-ray crystal structures of E. coli CheY.
| Structural description | PDB ID (chain) | State | Cα RMSD a |
β4α4 angle b | W58 χ2 | M85 χ1 | T87-D57 (Oγ1-Cγ) c | V86 Ψ | V86 Φ | Y106 χ1 | β5α5 angle d | K109-D12 (Nζ-Cγ) e | α1 to β5α5 (Cα-Cα) f |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CheY | 3CHY(A) | Inactive | - | 16.2 | −107.2 | −169.3 (−67.7) | 6.6 | 135.5 | −111.1 | 88.4 (179.9) | 160.3 | 5.0 | 5.3 |
| CheY A113P•Mg2+ | 3OO1(A) | Partially Active | 0.3 | 19.5 | −99.5 | −55.8 | 7.2 | 137.9 | −117.1 | 179.6 | 168.9 | 4.1 | 5.7 |
| CheY A113P•Mg2+ | 3OO1(B) | Partially Active | 0.4 | 7.9 h | −93.7 | −57.7 | 7.4 | 134.2 | −117.7 | 78.4 | 169.0 | 5.2 | 6.4 |
| CheY A113P•SO42−•Mn2+ | 3OO0(A) g | Partially Active | 0.6 | 110.3 (0.0; −45.1) i | −52.3 (−93.8) | −54.3 (−60.6) | 7.8 (5.3) j | 106.8 (129.2; 95.8) | −135.7 (−112.6; −117.5) | −163.8 (71.8) | 172.0 | 3.8 (5.2) | 6.4 |
| CheY A113P•SO42−Mn2+ | 3OO0(B) g | Partially Active | 0.5 | 109.3 | −49.5 | −55.7 | 5.4 | 104.0 | −134.9 | −159.5 | 171.7 | 3.8 | 6.5 |
| CheY A113P•BeF3−Mn2+ | 3MYY(A) | Active | 0.5 | 111.1 | −40.3 | −54.5 | 3.5 | 105.0 | −136.3 | −165.8 | 167.5 | 3.7 | 6.5 |
| CheY A113P•BeF3−Mn2+ | 3MYY(B) | Active | 0.5 | 111.8 | −36.3 | −55.8 | 3.4 | 109.0 | −132.0 | −157.3 | 168.2 | 3.7 | 6.5 |
| CheY•BeF3−Mn2+ | 1FQW(A) | Active | 0.5 | 109.3 | −45.2 | −57.6 | 3.6 | 100.4 | −137.4 | −164.2 | 173.6 | 3.8 | 6.7 |
| CheY•BeF3−Mn2+ | 1FQW(B) | Active | 0.5 | 110.5 | −40.3 | −55.5 | 3.4 | 100.2 | −138.4 | −160.1 | 169.1 | 3.8 | 6.5 |
| CheY•BeF3−Mg2+FliM1-16 | 1F4V(A) | Active | 0.5 | 112.8 | −50.1 | −54.0 | 3.5 | 106.4 | −133.9 | −156.4 | 169.8 | 3.7 | 6.8 |
| CheY•BeF3−Mg2+FliM1-16 | 1F4V(B) | Active | 0.5 | 113.1 | −57.1 | −56.0 | 3.4 | 94.2 | −143.3 | −155.3 | 168.5 | 3.6 | 6.6 |
| CheY•BeF3−Mg2+FliM1-16 | 1F4V(C) | Active | 0.8 | 102.9 | −53.8 | −52.4 | 3.8 | 102.2 | −130.0 | −156.2 | 162.0 | 4.0 | 6.6 |
Characteristics of inactive CheY are in orange and of active CheY are in purple.
CαRMSD representing atomic displacement between the reference structure (PDB ID: 3CHY) and the mobile structure.
Pseudo-dihedral angles were measured using Cα atoms for residues T87:A88:E89:A90 (β4α4 loop conformation). Measurements for alternate conformers are included in parentheses.
Interatomic distances were calculated from the Oγ1 atom of the T87 residue to Cγ of the D57 phosphorylation site. In structures with BeF3−, the Cγ atom was replaced with the Be atom for measurement.
Pseudo-dihedral angles were measured using Cα atoms for residues K109:P110:F111:T112 (β5α5 loop conformation). Measurements for alternate conformers are included in parentheses.
Interatomic distances were calculated from the terminal Nζ atom of K109 to Cγ of D12.
Interatomic distance between Cα atoms of residue 113 (β5α5 loop) and L24 (α1).
Structures include sulfate molecule(s) bound within the active site.
No density was observed for E89 side chain, suggesting high flexibility.
Residues T87:A88:E89:A90 are highly ambiguous in the 3OO0 protomer A. E89 accesses positions equivalent to those found in both the apo and BeF3− bound CheY structures.
A third conformer was observed for T87 in the 3OO0 protomer A, nearly identical to the primary conformer.