2QKX
N-acetyl glucosamine 1-phosphate uridyltransferase from Mycobacterium tuberculosis complex with N-acetyl glucosamine 1-phosphate
Summary for 2QKX
| Entry DOI | 10.2210/pdb2qkx/pdb |
| Descriptor | Bifunctional protein glmU, 2-acetamido-2-deoxy-1-O-phosphono-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | rossmann, beta-helix, substrate complex, structural genomics, tb structural genomics consortium, tbsgc, transferase |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): P96382 |
| Total number of polymer chains | 1 |
| Total formula weight | 41062.95 |
| Authors | Zhang, Z.,Squire, C.J.,Baker, E.N.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2007-07-11, release date: 2008-07-15, Last modification date: 2023-08-30) |
| Primary citation | Zhang, Z.,Bulloch, E.M.,Bunker, R.D.,Baker, E.N.,Squire, C.J. Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr.,Sect.D, 65:275-283, 2009 Cited by PubMed Abstract: Antibiotic resistance is a major issue in the treatment of infectious diseases such as tuberculosis. Existing antibiotics target only a few cellular pathways and there is an urgent need for antibiotics that have novel molecular mechanisms. The glmU gene is essential in Mycobacterium tuberculosis, being required for optimal bacterial growth, and has been selected as a possible drug target for structural and functional investigation. GlmU is a bifunctional acetyltransferase/uridyltransferase that catalyses the formation of UDP-GlcNAc from GlcN-1-P. UDP-GlcNAc is a substrate for two important biosynthetic pathways: lipopolysaccharide and peptidoglycan synthesis. The crystal structure of M. tuberculosis GlmU has been determined in an unliganded form and in complex with GlcNAc-1-P or UDP-GlcNAc. The structures reveal the residues that are responsible for substrate binding. Enzyme activities were characterized by (1)H NMR and suggest that the presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity. PubMed: 19237750DOI: 10.1107/S0907444909001036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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