6U78
Rv3722c in complex with glutamic acid
Summary for 6U78
| Entry DOI | 10.2210/pdb6u78/pdb |
| Descriptor | Aminotransferase, PYRIDOXAL-5'-PHOSPHATE, GLUTAMIC ACID, ... (6 entities in total) |
| Functional Keywords | aminotransferase, pyridoxal phosphate, complex, mycobacterium tuberculosis, transferase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 4 |
| Total formula weight | 190846.93 |
| Authors | Mandyoli, L.,Sacchettini, J.C. (deposition date: 2019-08-31, release date: 2020-05-06, Last modification date: 2023-10-11) |
| Primary citation | Jansen, R.S.,Mandyoli, L.,Hughes, R.,Wakabayashi, S.,Pinkham, J.T.,Selbach, B.,Guinn, K.M.,Rubin, E.J.,Sacchettini, J.C.,Rhee, K.Y. Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis. Nat Commun, 11:1960-1960, 2020 Cited by PubMed Abstract: Gene rv3722c of Mycobacterium tuberculosis is essential for in vitro growth, and encodes a putative pyridoxal phosphate-binding protein of unknown function. Here we use metabolomic, genetic and structural approaches to show that Rv3722c is the primary aspartate aminotransferase of M. tuberculosis, and mediates an essential but underrecognized role in metabolism: nitrogen distribution. Rv3722c deficiency leads to virulence attenuation in macrophages and mice. Our results identify aspartate biosynthesis and nitrogen distribution as potential species-selective drug targets in M. tuberculosis. PubMed: 32327655DOI: 10.1038/s41467-020-15876-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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