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Figure 1
Schematic representations of the SGSH structure. (a) Mapping of SGSH primary and secondary structures. β-Strands, red arrows; α-helices, blue striped rectangles; 310-helices, violet rectangles; the two disulfide bridges are shown as orange lines and the four glycosylated asparagines as yellow filled circles. Functionally important residues (active site and glycosylation sites) are shown in red; some of the residues at the dimer interface are shown in blue. The phenotype of the missense mutation sites is indicated below the sequence as follows: early-onset disease (E), red; intermediate-onset (I), orange; late-onset (L), blue; phenotype not reported in the literature (N), grey. (b) Topology diagram (not drawn to scale). Colour coding is similar to that in Fig. 1[link](a), with α-helices shown as blue cylinders and the N-terminus and C-terminus as blue and red circles, respectively. Divalent metal-binding residues are labelled M1 (Asp31, Asp32), M2 (FGly70) and M3 (Asp273, Asn274). Secondary-structure elements are named as indicated in the main text.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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