 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](gx5140fig1mag.jpg)
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Figure 1
(a) Native crystal of GlmU obtained using ammonium sulfate as a precipitant. The crystals, which were grown in a hanging-drop setup, grew to dimensions of ∼0.3 × 0.3 × 0.3 mm. (b) The structure of GlmU. Each monomer contains an N-terminal domain (coloured pink) responsible for the uridyltransferase activity and a C-terminal domain with a left-handed β-helix fold (LβH; coloured gold) responsible for acetyltransferase activity. A hinge helix (coloured blue) connects the two domains and the C-terminal extensions are marked red. (c) GlmU forms a biological trimer. Two of the three monomers of the trimer are coloured dark grey and light blue, while the other is coloured as in (b). The N- and C-terminal parts of the trimer are defined as the `head' and the `tail'. |
![[Figure 1]](gx5140fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
