2j9i
From Proteopedia
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| - | [[Image:2j9i.jpg|left|200px]] | + | [[Image:2j9i.jpg|left|200px]] |
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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.''' | + | {{Structure |
| + | |PDB= 2j9i |SIZE=350|CAPTION= <scene name='initialview01'>2j9i</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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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.''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2J9I is a [ | + | 2J9I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9I OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17161372 17161372] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:02 2008'' |
Revision as of 15:39, 20 March 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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