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Literature summary for 2.4.1.345 extracted from
- Molecular basis of membrane association by the phosphatidylinositol mannosyltransferase PimA enzyme from mycobacteria (2016), J. Biol. Chem., 291, 13955-13963.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycolicibacterium smegmatis | A0QWG6 | - |
- |
| Mycolicibacterium smegmatis ATCC 700084 | A0QWG6 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | PimA preferentially binds to negatively charged phosphatidyl-myo-inositol substrate and non-substrate membrane model systems (small unilamellar vesicle) through its N-terminal domain, inducing an important structural reorganization of anionic phospholipids. This interaction is mainly mediated by amphipathic helix alpha2, which undergoes a substantial conformational change and localizes in the vicinity of the negatively charged lipid headgroups and the very first carbon atoms of the acyl chains, at the PimA-phospholipid interface. A flexible region within the N-terminal domain undergoes beta-strand-to-alpha-helix and alpha-helix-to-beta-strand transitions during catalysis and interacts with anionic phospholipids, but the effect is markedly less pronounced to that observed for the amphipathic helix alpha2 | Mycolicibacterium smegmatis |
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Release 2023.1 (January 2023)
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