Structural highlights
Publication Abstract from PubMed
UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in pathogens by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose. Here we report the first crystal structure of a covalent intermediate in the UGM reaction. The 2.3 A resolution structure reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD.
In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.,Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ Biochemistry. 2016 Feb 16;55(6):833-6. doi: 10.1021/acs.biochem.6b00035. Epub, 2016 Feb 4. PMID:26836146[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ. In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction. Biochemistry. 2016 Feb 16;55(6):833-6. doi: 10.1021/acs.biochem.6b00035. Epub, 2016 Feb 4. PMID:26836146 doi:http://dx.doi.org/10.1021/acs.biochem.6b00035
