Selenocysteine synthase

Function

Selenocysteine synthase or O-phosphoseryl-tRNA(Sec) selenium transfrase (SecS) converts phospho-seryl-tRNA (tRNASec) into selenocysteinyl-tRNA using selenophosphate as the Se donor[1].

Disease

Mutations in SecS cause cerebello-cerebral atrophy[2].

Structural insights

The active site of SecS contains the , , and [3]. Water molecules are shown as red spheres.

Human selenocysteine synthase containing phosphoserine complex with tRNASec, monothiophosphate, deoxypyridoxine phosphate (PDB entry 3hl2)

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3D Structures of selenocysteine synthase3D Structures of selenocysteine synthase

Updated on 15-March-2022

4zdl – hSecS (mutant) - human
3hl2 - hSecS + tRNASec
4zdo, 4zdp – hSecS (mutant) + tRNASec
7l1t – hSecS + pyridoxine derivative
3bc8, 3bca - mSecS elastase-resistant fragment - mouse

3bcb - mSecS elastase-resistant fragment + phosphate

2z67 - SecS - Methanococcus maripaludis

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

ReferencesReferences

  1. 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
  2. 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
  3. Palioura S, Sherrer RL, Steitz TA, Soll D, Simonovic M. The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science. 2009 Jul 17;325(5938):321-5. PMID:19608919 doi:325/5938/321

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Michal Harel, Alexander Berchansky