Selenocysteine synthase
From Proteopedia
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{{STRUCTURE_2z67| PDB=2z67 | SIZE=400| SCENE= |right|CAPTION=Selenocysteine synthase tetramer complex with pyridoxal-5'-phosphate and sulfate, [[2z67]] }} | {{STRUCTURE_2z67| PDB=2z67 | SIZE=400| SCENE= |right|CAPTION=Selenocysteine synthase tetramer complex with pyridoxal-5'-phosphate and sulfate, [[2z67]] }} | ||
| - | + | == Function == | |
'''Selenocysteine synthase''' (SecS) converts phospho-seryl-tRNA into selenocysteinyl-tRNA using selenophosphate as the Se donor<ref>PMID:1839607</ref>. | '''Selenocysteine synthase''' (SecS) converts phospho-seryl-tRNA into selenocysteinyl-tRNA using selenophosphate as the Se donor<ref>PMID:1839607</ref>. | ||
| + | |||
| + | == Disease == | ||
| + | Mutations in SecS cause cerebello-cerebral atrophy<ref>PMID:21670677</ref>. | ||
== 3D Structures of selenocysteine synthase == | == 3D Structures of selenocysteine synthase == | ||
Revision as of 07:39, 24 August 2016
Contents |
Function
Selenocysteine synthase (SecS) converts phospho-seryl-tRNA into selenocysteinyl-tRNA using selenophosphate as the Se donor[1].
Disease
Mutations in SecS cause cerebello-cerebral atrophy[2].
3D Structures of selenocysteine synthase
Updated on 24-August-2016
3bc8, 3bca - mSecS elastase-resistant fragment - mouse
3bcb - mSecS elastase-resistant fragment + phosphate
2z67 - SecS - Methanococcus maripaludis
3hl2 - SecS + tRNASec - human
3w1i – AaSecS + pyridine derivative – Aquifex aeolicus
3wcn – AaSecS (mutant)
3w1h, 3wco – AaSecS (mutant) + pyridine derivative
3w1j – AaSecS + pyridine derivative
3w1k – AaSecS (mutant) + pyridine derivative + tRNASec
References
- ↑ Forchhammer K, Boesmiller K, Bock A. The function of selenocysteine synthase and SELB in the synthesis and incorporation of selenocysteine. Biochimie. 1991 Dec;73(12):1481-6. PMID:1839607
- ↑ Schweizer U, Dehina N, Schomburg L. Disorders of selenium metabolism and selenoprotein function. Curr Opin Pediatr. 2011 Aug;23(4):429-35. doi: 10.1097/MOP.0b013e32834877da. PMID:21670677 doi:http://dx.doi.org/10.1097/MOP.0b013e32834877da
