Abstract
GlmU is a bifunctional enzyme that catalyzes the final two steps in the biosynthesis of UDP-GlcNAc. Crystals of GlmU from Mycobacterium tuberculosis obtained using ammonium sulfate as a precipitant diffracted poorly (to 3.4 Å resolution) and displayed an unusually high solvent content (>80%) with sparse crystal packing that resulted in large solvent channels. With one molecule per asymmetric unit, the monomers from three neighbouring asymmetric units related by the crystal threefold formed a biological trimer. Although this is the first report of the structure of GlmU determined in a cubic crystal form, the trimeric arrangement here is similar to that observed for other GlmU structures determined in hexagonal (H3, H32, P6322) space groups.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 435-439 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 65 |
| Issue number | 5 |
| DOIs | |
| State | Published - 2009 |
| Externally published | Yes |
Keywords
- Acetyltransferases
- Bifunctional enzymes
- GlmU
- Mycobacterium tuberculosis
- Uridyltransferases
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Genetics
- Condensed Matter Physics