Preliminary crystallographic analysis of GpgS, a key glucosyltransferase involved in methylglucose lipopolysaccharide biosynthesis inMycobacterium tuberculosis
| Autor: | Mary Jackson, Marcelo E. Guerin, Patrick J. Brennan, Ha T. Pham, Mark J. van der Woerd, Emily Hansen, Devinder Kaur, Petra Gest |
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| Rok vydání: | 2008 |
| Předmět: |
Lipopolysaccharides
CAZy Biophysics macromolecular substances Crystallography X-Ray Biochemistry Uridine Diphosphate Mycobacterium tuberculosis chemistry.chemical_compound Bacterial Proteins Structural Biology Glycosyltransferase Genetics chemistry.chemical_classification ATP synthase biology fungi Glycosyltransferases Condensed Matter Physics biology.organism_classification carbohydrates (lipids) Uridine diphosphate Crystallography Enzyme chemistry Crystallization Communications biology.protein Glucosyltransferase Lipopolysaccharide Biosynthesis |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64:1121-1124 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309108032892 |
| Popis: | Glucosyl-3-phosphoglycerate synthase (GpgS) is a key enzyme that catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria. These important molecules are believed to be involved in the regulation of fatty-acid and mycolic acid synthesis. The enzyme belongs to the recently defined GT81 family of retaining glycosyltransferases (CAZy, Carbohydrate-Active Enzymes Database; see http://www.cazy.org). Here, the purification, crystallization and preliminary crystallographic analysis are reported of GpgS from Mycobacterium tuberculosis and of its complex with UDP. GpgS crystals belonged to space group I4, with unit-cell parameters a = 98.85, b = 98.85, c = 127.64 A, and diffracted to 2.6 A resolution. GpgS-UDP complex crystals belonged to space group I4, with unit-cell parameters a = 98.32, b = 98.32, c = 127.96 A, and diffracted to 3.0 A resolution. |
| Databáze: | OpenAIRE |
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