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Fig. 1 | Orphanet Journal of Rare Diseases

Fig. 1

From: Clinical and molecular characterization of patients with adenylosuccinate lyase deficiency

Fig. 1

Sequence alignments and location of the mutated residues in the identified ADSL holoenzyme organization. (top) Multiple sequence alignments around the residues affected by the previously unreported ADSL mutations (columns with invariant residues are grayed). (bottom) Crystal structure of the ADSL homotetramer (PDB 2VD6) showing the amino acids hit by mutations (the residues affected by the novel mutations presented in this study are highlighted by a red surface, those affected by previously reported a blue surface highlights mutations; all mutation sites are mapped on the same monomer; the four monomers are in different ribbon colors). The co-crystallized substrate and its enzymatic products (adenylosuccinic acid, ASA, green sticks; adenosine monophosphate, AMP, yellow sticks; fumaric acid, FA, magenta sticks) are also shown. The closed-up views highlight structural details around the sites involved by the novel mutations (including the known mutations falling nearby). For better clarity of visualization of the residues, enlarged views are oriented differently from the whole structure. Amino acid numbering of ADSL protein refers to the NCBI protein entry NP_000017.1

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