1h7q: Difference between revisions

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.

1H7Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MN, MG and TYD as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H7Q OCA].  

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