1H7L

dTDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS

Summary for 1H7L

• Entry DOI: 10.2210/pdb1h7l/pdb
• Related: 1H7Q 1QG8 1QGQ 1QGS
• Descriptor: SPORE COAT POLYSACCHARIDE BIOSYNTHESIS PROTEIN SPSA, MAGNESIUM ION, THYMIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase, glycosyltransferase
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 30541.73

Authors

Tarbouriech, N.,Charnock, S.J.,Davies, G.J. (deposition date: 2001-07-09, release date: 2001-12-13, Last modification date: 2024-10-16)

Primary citation

Tarbouriech, N.,Charnock, S.J.,Davies, G.J.
Three-Dimensional Structures of the Mn and Mg Dtdp Complexes of the Family Gt-2 Glycosyltransferase Spsa: A Comparison with Related Ndp-Sugar Glycosyltransferases.
J.Mol.Biol., 314:655-, 2001

PubMed Abstract: The vast majority of glycosidic-bond synthesis in nature is performed by glycosyltransferases, which use activated glycosides as the sugar donor. Typically, the activated leaving group is a nucleoside phosphate, lipid phosphate or phosphate. The nucleotide-sugar-dependent glycosyltransferases fall into over 50 sequence-based families, with the largest and most widespread family of inverting transferases named family GT-2. Here, we present the three-dimensional crystal structure of SpsA, the first and currently the only structural representative from family GT-2, in complex with both Mn-dTDP and Mg-dTDP at a resolution of 2 A. These structures reveal how SpsA and related enzymes may display nucleotide plasticity and permit a comparison of the catalytic centre of this enzyme with those from related sequence families whose three-dimensional structures have recently been determined. Family GT-2 enzymes, together with enzymes from families 7, 13 and 43, appear to form a clan of related structures with identical catalytic apparatus and reaction mechanism.

PubMed: 11733986
DOI: 10.1006/JMBI.2001.5159

Experimental method

X-RAY DIFFRACTION (1.98 Å)