Crystal Structure Analysis of the Polysialic Acid Specific O-Acetyltransferase NeuO
Figure 3
(A) The active and polySia binding site of NeuO is displayed as a full molecule view with half-transparent surface for two chains (right panel). A close-up view shows the binding site in detail (left panel). Residues that are conserved between NeuO and the closely related O-acetyltransferase OatWY are underlined and shown in ball and stick mode. In addition, residues that form the proposed polySia binding site are highlighted in ball and stick mode. The donor-substrate acetyl-CoA (shown as green sticks) was modeled into the NeuO structure by superposition with the crystal structure of the acetyltransferase OatWY (PDB-ID: 2WLF) from N. meningitidis. (B) A rotation of 45° allows a better view into the active site located at the interface of two adjacent subunits and shows the close proximity of Met134 and Trp171 belonging to the same subunit and His147, which belongs to the adjacent monomer.