1qgs
From Proteopedia
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UDP-MAGNESIUM COMPLEX OF SPSA FROM BACILLUS SUBTILIS
Overview
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.
About this Structure
1QGS is a Single protein structure of sequence from Bacillus subtilis with MG, UDP and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms., Charnock SJ, Davies GJ, Biochemistry. 1999 May 18;38(20):6380-5. PMID:10350455
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