4WAD
Crystal Structure of TarM with UDP-GlcNAc
Summary for 4WAD
| Entry DOI | 10.2210/pdb4wad/pdb |
| Descriptor | Glycosyl transferase, group 1 family protein, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | gt-b fold, gt-4, retaining glycosyltransferase, duf1975, rossmann fold, wta-binding, transferase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 58739.72 |
| Authors | Koc, C.,Stehle, T.,Xia, G.,Peschel, A. (deposition date: 2014-08-29, release date: 2015-02-25, Last modification date: 2024-01-10) |
| Primary citation | Koc, C.,Gerlach, D.,Beck, S.,Peschel, A.,Xia, G.,Stehle, T. Structural and Enzymatic Analysis of TarM Glycosyltransferase from Staphylococcus aureus Reveals an Oligomeric Protein Specific for the Glycosylation of Wall Teichoic Acid. J.Biol.Chem., 290:9874-9885, 2015 Cited by PubMed Abstract: Anionic glycopolymers known as wall teichoic acids (WTAs) functionalize the peptidoglycan layers of many Gram-positive bacteria. WTAs play central roles in many fundamental aspects of bacterial physiology, and they are important determinants of pathogenesis and antibiotic resistance. A number of enzymes that glycosylate WTA in Staphylococcus aureus have recently been identified. Among these is the glycosyltransferase TarM, a component of the WTA de novo biosynthesis pathway. TarM performs the synthesis of α-O-N-acetylglycosylated poly-5'-phosphoribitol in the WTA structure. We have solved the crystal structure of TarM at 2.4 Å resolution, and we have also determined a structure of the enzyme in complex with its substrate UDP-GlcNAc at 2.8 Å resolution. The protein assembles into a propeller-like homotrimer in which each blade contains a GT-B-type glycosyltransferase domain with a typical Rossmann fold. The enzymatic reaction retains the stereochemistry of the anomeric center of the transferred GlcNAc-moiety on the polyribitol backbone. TarM assembles into a trimer using a novel trimerization domain, here termed the HUB domain. Structure-guided mutagenesis experiments of TarM identify residues critical for enzyme activity, assign a putative role for the HUB in TarM function, and allow us to propose a likely reaction mechanism. PubMed: 25697358DOI: 10.1074/jbc.M114.619924 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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