TABLE 2.
Residues involved in the interaction of EIIAGlc with partner proteinsa
| Partner protein | Interface residue(s) of:
|
Reference(s) | |
|---|---|---|---|
| Partner protein | EIIAGlc | ||
| HPr active site | His-15, Arg-17 | His-90,b His-75b | 330, 941 (HPr); 197, 686 (EIIAGlc) |
| Interaction surface | Arg-17, Lys-24, Lys-27, Lys-49 | Val-40, Phe-41, Val-46, Phe-71, Phe-88, Val-96, Lys-69 (aliphatic side chain), Asp-38,c Glu-72, Glu-80, Glu-86; Asp-94,c Glu-97, Glu-109, Asp-144, Ser-78, Ser-141 | 929 |
| EIICBGlc active site | Cys-421, Arg-424, Arg-426 | 449, 547 | |
| Interaction surface | Arg-424,d Arg-426,d Lys-467, Asp-419; Asp-464 | Val-40, Phe-41, Val-46, Phe-71,e Phe-88, Val-96, Lys-69,e Lys-99,e Asp-38, Glu-72; Asp-94, Glu-97; Ser-141 | 98 |
| GlpK (E. coli) interaction surface | Residues 472-481 | Val-40, Phe-41, Val-46, Phe-71, Phe-88, Val-96, Lys-69, Lys-99, Asp-38, Glu-72; Glu-92, Asp-94, Asp-97 | 355 |
| Cofactor Zn2+ | Glu-478 | His-75, His-90 | 223 |
| LacY interaction surface | Val-132, Pro-192, Val-197, Ala-198, Arg-135, Arg-142, Ser-133, Thr-196, Asn-199, Ser-202, Asn-204, Ser-206 | Gly-47, Phe-71, Ala-76, Lys-69, Glu-86; Asp-94, Ser-78 | 338, 823, 951 (LacY); 987 (EIIA) |
| MelB interaction surface | Ile-445, Asp-438, Asp-441; Asp-449, Arg-452 | 439, 440 | |
| MalK interaction surface | Ala-124, Phe-241, Gly-278, Gly-284, Gly-302, Arg-228, Glu-119, Ser-322 | 167, 431 | |
a
The active-site residues are indicated by boldface type.
b
His-68 and His-83 in B. subtilis (124).
c
Asp-31 and Asp-87 in B. subtilis (124).
d
Arg-38 and Arg-40 of the E. coli EIIBGlc domain (270).
e
Point mutations that block P transfer to HPr and/or EIICBGlc are Lys69Leu, Lys69Glu, Lys99Glu, Phe71Leu, and Phe71Ser (822).