1QGS
UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS
Summary for 1QGS
| Entry DOI | 10.2210/pdb1qgs/pdb |
| Related | 1QG8 1QGQ |
| Descriptor | PROTEIN (SPORE COAT POLYSACCHARIDE BIOSYNTHESIS PROTEIN SPSA), MAGNESIUM ION, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | glycosyltransferase, transferase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 30635.80 |
| Authors | Charnock, S.J. (deposition date: 1999-05-04, release date: 2000-05-04, Last modification date: 2024-10-16) |
| Primary citation | Charnock, S.J.,Davies, G.J. Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry, 38:6380-6385, 1999 Cited by PubMed Abstract: The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosyl moiety from an activated nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a glycosyltransferase implicated in the synthesis of the spore coat of Bacillus subtilis, whose homologues include cellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensional crystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 A. It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domain which features a disordered loop spanning the active site. The structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 A, respectively. These complexes, together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous family of inverting glycosyltransferases. PubMed: 10350455DOI: 10.1021/bi990270y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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