Publication details
Substrate translocation in processive glycosyltransferase GlfT2
| Authors | |
|---|---|
| Year of publication | 2018 |
| Type | Appeared in Conference without Proceedings |
| Citation | |
| Description | Glycosyltransferases are enzymes that catalyze the transfer of saccharide units and the formation of glycosidic bonds. Galactofuranosyltransferase 2 (GlfT2) is a key glycosyltransferase from Mycobacterium Tuberculosis. It catalyzes the transfer of galactofuranosyl (Galf) unit from donor substrate UDP-Galf onto a growing polysaccharide chain in alternating ß-(1-5) or ß-(1-6) linkages. The resulting galactan is a key part of the mycobacterial cell wall. GlfT2 is an interesting glycosyltransferase from a mechanistic point of view as well. It has a dual activity and works in processive manner switching the ß-(1-5) or ß-(1-6) mechanisms between steps. We have previously studied the two mechanisms using QM/MM Ab Initio MD coupled with metadynamics and string method. We have found very little difference between the two mechanisms. Now we turn our attention onto the process of translocation of the bound substrate between the rounds of glycosyltransferase activity. The goal is to study the substrate translocation after the ß-(1-5) Galf addition and ß-(1-6) Galf addition. Identifing any differences between the two would help us understand the function of GlfT2 and how it regulates between the two mechanisms. We are using the transition path sampling methodology as implemented in OpenPathSampling package for this study. |