3FGP
2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations
Summary for 3FGP
| Entry DOI | 10.2210/pdb3fgp/pdb |
| Related | 3DKI |
| Descriptor | Cysteine synthase B (2 entities in total) |
| Functional Keywords | cysteine synthase, cysm, tuberculosis, cyso, o-phosphoserine, amino-acid biosynthesis, cysteine biosynthesis, pyridoxal phosphate, transferase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 2 |
| Total formula weight | 69904.47 |
| Authors | Agren, D.,Schnell, R.,Schneider, G. (deposition date: 2008-12-08, release date: 2008-12-23, Last modification date: 2023-11-22) |
| Primary citation | Agren, D.,Schnell, R.,Schneider, G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity Febs Lett., 583:330-336, 2009 Cited by PubMed Abstract: A new crystal structure of the dimeric cysteine synthase CysM from Mycobacterium tuberculosis reveals an open and a closed conformation of the enzyme. In the closed conformation the five carboxy-terminal amino acid residues are inserted into the active site cleft. Removal of this segment results in a decreased lifetime of the alpha-aminoacrylate reaction intermediate, an increased sensitivity to oxidants such as hydrogen peroxide, and loss of substrate selectivity with respect to the sulfur carrier thiocarboxylated CysO. These results highlight features of CysM that might be of particular importance for cysteine biosynthesis under oxidative stress in M. tuberculosis. PubMed: 19101553DOI: 10.1016/j.febslet.2008.12.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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