2aev
From Proteopedia
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|PDB= 2aev |SIZE=350|CAPTION= <scene name='initialview01'>2aev</scene>, resolution 2.00Å | |PDB= 2aev |SIZE=350|CAPTION= <scene name='initialview01'>2aev</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mj0158 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | |GENE= mj0158 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2aev|2AEV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aev OCA], [http://www.ebi.ac.uk/pdbsum/2aev PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aev RCSB]</span> | ||
}} | }} | ||
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[[Category: Rother, M.]] | [[Category: Rother, M.]] | ||
[[Category: Wahl, M C.]] | [[Category: Wahl, M C.]] | ||
| - | [[Category: SO4]] | ||
[[Category: homo-oligomerization]] | [[Category: homo-oligomerization]] | ||
[[Category: plp]] | [[Category: plp]] | ||
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[[Category: selenocysteine synthase]] | [[Category: selenocysteine synthase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:44 2008'' |
Revision as of 22:51, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mj0158 (Methanocaldococcus jannaschii) | ||||||
| Related: | 2AEV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MJ0158, NaBH4-reduced form
Overview
Bacterial selenocysteine synthase converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) for selenoprotein biosynthesis. The identity of this enzyme in archaea and eukaryotes is unknown. On the basis of sequence similarity, a conserved open reading frame has been annotated as a selenocysteine synthase gene in archaeal genomes. We have determined the crystal structure of the corresponding protein from Methanococcus jannaschii, MJ0158. The protein was found to be dimeric with a distinctive domain arrangement and an exposed active site, built from residues of the large domain of one protomer alone. The shape of the dimer is reminiscent of a substructure of the decameric Escherichia coli selenocysteine synthase seen in electron microscopic projections. However, biochemical analyses demonstrated that MJ0158 lacked affinity for E. coli seryl-tRNA(Sec) or M. jannaschii seryl-tRNA(Sec), and neither substrate was directly converted to selenocysteinyl-tRNA(Sec) by MJ0158 when supplied with selenophosphate. We then tested a hypothetical M. jannaschii O-phosphoseryl-tRNA(Sec) kinase and demonstrated that the enzyme converts seryl-tRNA(Sec) to O-phosphoseryl-tRNA(Sec) that could constitute an activated intermediate for selenocysteinyl-tRNA(Sec) production. MJ0158 also failed to convert O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). In contrast, both archaeal and bacterial seryl-tRNA synthetases were able to charge both archaeal and bacterial tRNA(Sec) with serine, and E. coli selenocysteine synthase converted both types of seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). These findings demonstrate that a number of factors from the selenoprotein biosynthesis machineries are cross-reactive between the bacterial and the archaeal systems but that MJ0158 either does not encode a selenocysteine synthase or requires additional factors for activity.
About this Structure
2AEV is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Structural and functional investigation of a putative archaeal selenocysteine synthase., Kaiser JT, Gromadski K, Rother M, Engelhardt H, Rodnina MV, Wahl MC, Biochemistry. 2005 Oct 11;44(40):13315-27. PMID:16201757
Page seeded by OCA on Mon Mar 31 01:51:44 2008
