EC Number   |
Subunits |
Reference |
|---|
   2.3.1.4 | ? |
x * 19400, SDS-PAGE, mutant Q155V/C158G and wild-type |
757601 |
| 2.3.1.4 | ? |
x * 21000, SDS-PAGE, immunoblotting, deduced from nucleotide sequence |
486909 |
| 2.3.1.4 | ? |
x * 52000, SDS-PAGE |
719137 |
| 2.3.1.4 | dimer |
2 * 19200, calculated, 2 * 20000, SDS-PAGE |
718794 |
| 2.3.1.4 | dimer |
2 * 25000, SDS-PAGE |
671094 |
| 2.3.1.4 | dimer |
and monomer, 2 * 19400, SDS-PAGE |
757601 |
| 2.3.1.4 | dimer |
HsGNA1 forms a tight dimer shown by crystal structure analysis: Each monomer is composed of 184 residues and the monomer structure belongs to a classic GNAT fold of a/b protein, containing all four motifs (C, D, A and B) conserved among the GNATs. Motif C (b1, g2 and a2) and Motif D (b2 and b3) are located next to and interact with each other, contributing to the hydrophobic core. Motif B (b5 and a5) make up part of the active site. Strands b1-b4 form an antiparallel beta sheet, and helices a1-a4, g1 and g2 are flanked on both sides of the central beta sheet. The HsGNA1 dimer is constructed by joining two subunits such that the C-terminal strand b6 projects to the other subunit. The b6-strand swaps between subunits in a dimer. The loop between strands b3 and b4 also extends to the other subunit, contributing to GlcN6P binding. In each subunit, the AcCoA binding cleft is formed by the diverging strands b4 and b5 |
686767 |
| 2.3.1.4 | homodimer |
crystal structure |
685012 |
