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1h7l
From Proteopedia
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DTDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS
Overview
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.
About this Structure
1H7L is a Single protein structure of sequence from Bacillus subtilis with MG and TYD as ligands. Structure known Active Site: TYD. Full crystallographic information is available from OCA.
Reference
Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases., Tarbouriech N, Charnock SJ, Davies GJ, J Mol Biol. 2001 Dec 7;314(4):655-61. PMID:11733986
Page seeded by OCA on Mon Nov 5 16:31:30 2007
