2j9i
From Proteopedia
(New page: 200px<br /><applet load="2j9i" size="350" color="white" frame="true" align="right" spinBox="true" caption="2j9i" /> '''LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY O...) |
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==Overview== | ==Overview== | ||
| - | Lengsin is a major protein of the vertebrate eye lens. It belongs to 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bateman, O | + | [[Category: Bateman, O A.]] |
| - | [[Category: Orlova, E | + | [[Category: Orlova, E V.]] |
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: Wang, L.]] | [[Category: Wang, L.]] | ||
| - | [[Category: White, H | + | [[Category: White, H E.]] |
[[Category: Wistow, G.]] | [[Category: Wistow, G.]] | ||
[[Category: Wyatt, K.]] | [[Category: Wyatt, K.]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:44 2008'' |
Revision as of 16:00, 21 February 2008
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LENGSIN IS A SURVIVOR OF AN ANCIENT FAMILY OF CLASS I GLUTAMINE SYNTHETASES IN EUKARYOTES THAT HAS UNDERGONE EVOLUTIONARY RE-ENGINEERING FOR A TISSUE-SPECIFIC ROLE IN THE VERTEBRATE EYE LENS.
Overview
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.
About this Structure
2J9I is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Lengsin is a survivor of an ancient family of class I glutamine synthetases re-engineered by evolution for a role in the vertebrate lens., Wyatt K, White HE, Wang L, Bateman OA, Slingsby C, Orlova EV, Wistow G, Structure. 2006 Dec;14(12):1823-34. PMID:17161372
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