 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](us5147fig1mag.jpg)
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Figure 1
The structure and sequence of LcGNAT is conserved among polyamine acetyltransferases. (a) Crystal structure of LcGNAT. Catalytic residues that are subjected to mutagenesis in this study are displayed. The P-loop is also highlighted. (b) Sequence alignment of LcGNAT and its four closest homologs with known 3D structures. The sequences correspond to Bacillus subtilis PaiA (BsPaiA), Streptococcus mutans putative acetyltransferase (SmGNAT), Thermoplasma acidophilum PaiA (TaPaiA) and T. volcanium N-acetyltransferase (TvArd1). PDB codes are given in parentheses. Residue numbering uses the LcGNAT sequence. Secondary structure is colour-coded as in (a), where β-strands are shown in green and α-helices are in yellow. Heavy outlined β-strands indicate the two strands involved in the formation of the V-shaped splay. Sequence identity is shown in yellow. Ac-CoA-binding residues were defined by PDB sequence annotations and are shown in green. The P-loop is boxed. Black dots indicate residues that are part of the substrate tunnel. Red stars highlight residues that were mutated in the acetylation activity assay. |
![[Figure 1]](us5147fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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