Figure 6
Comparison of the active site of GTFA-[Delta]N (blue, catalytic domain A; green, domain B) and GTF180-[Delta]N. Relevant residues from GTFA-[Delta]N are shown with blue or green C atoms and black labels and residues from GTF180-[Delta]N are shown with white C atoms and grey labels. (a) Superposition of GTFA-[Delta]N with the GTF180-[Delta]N D1025N-sucrose complex (subsites -1 and +1; PDB entry 3hz3 ; Vujicic-Zagar et al., 2010BB29). The three catalytic residues and the tyrosine residue below subsite -1 are shown in stick representation. The sucrose bound to GTF180-[Delta]N is shown with yellow C atoms. (b) Superposition of GTFA-[Delta]N with the GTF180-[Delta]N-maltose complex (subsites +1 and +2; PDB entry 3kll ; Vujicic-Zagar et al., 2010BB29). Maltose from the GTF180-[Delta]N complex, with its reducing-end glucosyl unit (subsite +2) stacking with a conserved tryptophan residue, is shown with yellow C atoms. The O1 atom of the acceptor sugar residue, which possibly interacts with Asn1134 in GTFA-[Delta]N, is indicated with an asterisk (*).  [article HTML]

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