Selenocysteine lyase

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== Structural highlights ==
== Structural highlights ==
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Rat SCL structure shows the <scene name='80/800703/Cv/3'>PLP moiety</scene> and bound L-cysteine within the active site cavity. The <scene name='80/800703/Cv/4'>cysteine carboxyl end forms salt bridge with SCL Arg and 2 hydrogen bonds with Ser and Asn while its amino group forms 2 hydrogen bonds with Ser and Ala</scene><ref>PMID:20164179</ref>.
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Rat SCL structure shows the <scene name='80/800703/Cv/7'>PLP moiety</scene> and bound L-cysteine within the active site cavity. The <scene name='80/800703/Cv/8'>cysteine carboxyl end forms salt bridge with SCL Arg and 2 hydrogen bonds with Ser and Asn while its amino group forms 2 hydrogen bonds with Ser and Ala</scene><ref>PMID:20164179</ref>. Water molecules are shown as red spheres.
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*<scene name='80/800703/Cv/5'>PLP interactions</scene>.
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*<scene name='80/800703/Cv/9'>PLP interactions</scene>.
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*<scene name='80/800703/Cv/6'>Whole active site</scene>.
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*<scene name='80/800703/Cv/10'>Whole active site</scene>.
</StructureSection>
</StructureSection>

Revision as of 13:50, 2 September 2019

Rat selenocysteine lyase complex with PLP, cysteine, phosphate and glycerol (PDB code 3a9y)

Drag the structure with the mouse to rotate

3D structures of selenocysteine lyase

Updated on 02-September-2019

1jf9, 1c0n - EcCsdB + PLP - Escherichia coli
1kmj, 1kmk - EcCsdB + PLP + cysteine derivative
5ft4, 5ft5, 5ft6 - EcCsdA + PLP
1i29 - EcCsdB + PLP + propagylglycine
5ft8 - EcCsdA + CsdE + PLP
3gzc, 3gzd - hSCL + PLP derivative - human
3a9x - rSCL + PLP - rat
3a9z - rSCL + PLP + selenopropionate
3a9y - rSCL + PLP + cysteine
4q75 - AtSCL + PLP derivative + cysteine derivative - Arabidopsis thaliana
4q76 - AtSCL (mutant) + PLP derivative + cysteine derivative

References

  1. ↑ Esaki N, Nakamura T, Tanaka H, Soda K. Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. J Biol Chem. 1982 Apr 25;257(8):4386-91. PMID:6461656
  2. ↑ Stadtman TC. Selenocysteine Lyase. EcoSal Plus. 2004 Dec;1(1). doi: 10.1128/ecosalplus.3.6.1.1.1. PMID:26443359 doi:http://dx.doi.org/10.1128/ecosalplus.3.6.1.1.1
  3. ↑ Seale LA, Hashimoto AC, Kurokawa S, Gilman CL, Seyedali A, Bellinger FP, Raman AV, Berry MJ. Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice. Mol Cell Biol. 2012 Oct;32(20):4141-54. doi: 10.1128/MCB.00293-12. Epub 2012 Aug , 13. PMID:22890841 doi:http://dx.doi.org/10.1128/MCB.00293-12
  4. ↑ Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N. Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase. J Biol Chem. 2010 Apr 16;285(16):12133-9. Epub 2010 Feb 17. PMID:20164179 doi:10.1074/jbc.M109.084475

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Michal Harel, Alexander Berchansky

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