+Search query
-Structure paper
Title | Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. |
---|---|
Journal, issue, pages | Structure, Vol. 14, Issue 12, Page 1823-1834, Year 2006 |
Publish date | Feb 1, 2007 |
Authors | Keith Wyatt / Helen E White / Luchun Wang / Orval A Bateman / Christine Slingsby / Elena V Orlova / Graeme Wistow / |
PubMed Abstract | Lengsin is a major protein of the vertebrate eye lens. It belongs to the hitherto purely prokaryotic GS I branch of the glutamine synthetase (GS) superfamily, but has no enzyme activity. Like the ...Lengsin is a major protein of the vertebrate eye lens. It belongs to the hitherto purely prokaryotic GS I branch of the glutamine synthetase (GS) superfamily, but has no enzyme activity. Like the taxon-specific crystallins, Lengsin is the result of the recruitment of an ancient enzyme to a noncatalytic role in the vertebrate lens. Cryo-EM and modeling studies of Lengsin show a dodecamer structure with important similarities and differences with prokaryotic GS I structures. GS homology regions of Lengsin are well conserved, but the N-terminal domain shows evidence of dynamic evolutionary changes. Compared with birds and fish, most mammals have an additional exon corresponding to part of the N-terminal domain; however, in human, this is a nonfunctional pseudoexon. Genes related to Lengsin are also present in the sea urchin, suggesting that this branch of the GS I family, supplanted by GS II enzymes in vertebrates, has an ancient role in metazoans. |
External links | Structure / PubMed:17161372 / PubMed Central |
Methods | EM (single particle) |
Resolution | 17.0 Å |
Structure data | EMDB-1290: Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens. |
Source |
|
Keywords | LIGASE |