2GEK
Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP
Summary for 2GEK
| Entry DOI | 10.2210/pdb2gek/pdb |
| Related | 2GEJ |
| Descriptor | PHOSPHATIDYLINOSITOL MANNOSYLTRANSFERASE (PimA), GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | gt4 glycosyltransferase, mannosyltransferase, rossmann fold, binary complex, transferase |
| Biological source | Mycobacterium smegmatis |
| Cellular location | Cell membrane; Single-pass membrane protein (Potential): A0QWG6 |
| Total number of polymer chains | 1 |
| Total formula weight | 43883.49 |
| Authors | Guerin, M.E.,Buschiazzo, A.,Kordulakova, J.,Jackson, M.,Alzari, P.M. (deposition date: 2006-03-20, release date: 2007-04-03, Last modification date: 2024-02-14) |
| Primary citation | Guerin, M.E.,Kordulakova, J.,Schaeffer, F.,Svetlikova, Z.,Buschiazzo, A.,Giganti, D.,Gicquel, B.,Mikusova, K.,Jackson, M.,Alzari, P.M. Molecular recognition and interfacial catalysis by the essential phosphatidylinositol mannosyltransferase PimA from mycobacteria. J.Biol.Chem., 282:20705-20714, 2007 Cited by PubMed Abstract: Mycobacterial phosphatidylinositol mannosides (PIMs) and metabolically derived cell wall lipoglycans play important roles in host-pathogen interactions, but their biosynthetic pathways are poorly understood. Here we focus on Mycobacterium smegmatis PimA, an essential enzyme responsible for the initial mannosylation of phosphatidylinositol. The structure of PimA in complex with GDP-mannose shows the two-domain organization and the catalytic machinery typical of GT-B glycosyltransferases. PimA is an amphitrophic enzyme that binds mono-disperse phosphatidylinositol, but its transferase activity is stimulated by high concentrations of non-substrate anionic surfactants, indicating that the early stages of PIM biosynthesis involve lipid-water interfacial catalysis. Based on structural, calorimetric, and mutagenesis studies, we propose a model wherein PimA attaches to the membrane through its N-terminal domain, and this association leads to enzyme activation. Our results reveal a novel mode of phosphatidylinositol recognition and provide a template for the development of potential antimycobacterial compounds. PubMed: 17510062DOI: 10.1074/jbc.M702087200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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