TABLE 2.

Residues involved in the interaction of EIIAGlc with partner proteinsa

Partner proteinInterface residue(s) of:Reference(s)
Partner proteinEIIAGlc
HPr active siteHis-15, Arg-17His-90,b His-75b330, 941 (HPr); 197, 686 (EIIAGlc)
Interaction surfaceArg-17, Lys-24, Lys-27, Lys-49Val-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-141929
EIICBGlc active siteCys-421, Arg-424, Arg-426449, 547
Interaction surfaceArg-424,d Arg-426,d Lys-467, Asp-419; Asp-464Val-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-14198
GlpK (E. coli) interaction surfaceResidues 472-481Val-40, Phe-41, Val-46, Phe-71, Phe-88, Val-96, Lys-69, Lys-99, Asp-38, Glu-72; Glu-92, Asp-94, Asp-97355
Cofactor Zn2+Glu-478His-75, His-90223
LacY interaction surfaceVal-132, Pro-192, Val-197, Ala-198, Arg-135, Arg-142, Ser-133, Thr-196, Asn-199, Ser-202, Asn-204, Ser-206Gly-47, Phe-71, Ala-76, Lys-69, Glu-86; Asp-94, Ser-78338, 823, 951 (LacY); 987 (EIIA)
MelB interaction surfaceIle-445, Asp-438, Asp-441; Asp-449, Arg-452439, 440
MalK interaction surfaceAla-124, Phe-241, Gly-278, Gly-284, Gly-302, Arg-228, Glu-119, Ser-322167, 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).