Crystallization (Comment) | Organism |
---|---|
hanging-drop vapour diffusion method at 20°C, three-dimensional structure of the apoenzyme, as well as of its ternary complex with UDP and 3-phosphoglycerate is determined by X-ray crystallography, to a resolution of 2.5 and 2.7 A, respectively | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-glucose + 3-phospho-D-glycerate | three-dimensional structures provide a molecular explanation for the enzymes preference for UDP-containing donor substrates, as well as for its glucose versus mannose discrimination, and uncover the structural determinants for acceptor substrate selectivity | Mycobacterium tuberculosis | UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
GpgS | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
physiological function | the increased resilience of this pathogen is due, to a great extent, to its complex, polysaccharide-rich, and unusually impermeable cell wall. Enzymes involved in glycosidic bond synthesis represent more than 1% of all ORFs identified from Mycobacterium tuberculosis. One of them is GpgS, a retaining glycosyltransferase with low sequence homology to any other glycosyltransferases of known structure, which has been identified in two species of mycobacteria and shown to be essential for the survival of Mycobacterium tuberculosis | Mycobacterium tuberculosis |