2Q74
Mycobacterium tuberculosis SuhB
Summary for 2Q74
| Entry DOI | 10.2210/pdb2q74/pdb |
| Descriptor | Inositol-1-monophosphatase (2 entities in total) |
| Functional Keywords | alpha-beta-alpha-beta-alpha sandwich, hydrolase |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 3 |
| Total formula weight | 93603.65 |
| Authors | Brown, A.K.,Meng, G.,Ghadbane, H.,Besra, G.S.,Futterer, K. (deposition date: 2007-06-06, release date: 2007-10-23, Last modification date: 2023-08-30) |
| Primary citation | Brown, A.K.,Meng, G.,Ghadbane, H.,Scott, D.J.,Dover, L.G.,Nigou, J.,Besra, G.S.,Futterer, K. Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+ Bmc Struct.Biol., 7:55-55, 2007 Cited by PubMed Abstract: The cell wall of Mycobacterium tuberculosis contains a wide range of phosphatidyl inositol-based glycolipids that play critical structural roles and, in part, govern pathogen-host interactions. Synthesis of phosphatidyl inositol is dependent on free myo-inositol, generated through dephosphorylation of myo-inositol-1-phosphate by inositol monophosphatase (IMPase). Human IMPase, the putative target of lithium therapy, has been studied extensively, but the function of four IMPase-like genes in M. tuberculosis is unclear. PubMed: 17725819DOI: 10.1186/1472-6807-7-55 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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