|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Methanococcus jannacshii O-phosphoseryl-tRNA synthetase== | | ==Crystal structure of Methanococcus jannacshii O-phosphoseryl-tRNA synthetase== |
| - | <StructureSection load='2du7' size='340' side='right' caption='[[2du7]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <StructureSection load='2du7' size='340' side='right'caption='[[2du7]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2du7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DU7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2du7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DU7 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2du3|2du3]], [[2du4|2du4]], [[2du5|2du5]], [[2du6|2du6]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2du7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2du7 OCA], [http://pdbe.org/2du7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2du7 RCSB], [http://www.ebi.ac.uk/pdbsum/2du7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2du7 ProSAT], [http://www.topsan.org/Proteins/RSGI/2du7 TOPSAN]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2du7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2du7 OCA], [https://pdbe.org/2du7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2du7 RCSB], [https://www.ebi.ac.uk/pdbsum/2du7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2du7 ProSAT], [https://www.topsan.org/Proteins/RSGI/2du7 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SEPS_METJA SEPS_METJA]] Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).<ref>PMID:15790858</ref> | + | [https://www.uniprot.org/uniprot/SEPS_METJA SEPS_METJA] Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).<ref>PMID:15790858</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 30: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]] | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43067]] | + | [[Category: Large Structures]] |
| - | [[Category: Fukunaga, R]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Structural genomic]] | + | [[Category: Fukunaga R]] |
| - | [[Category: Alpha4 tetramer]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
SEPS_METJA Catalyzes the attachment of O-phosphoserine (Sep) to tRNA(Cys).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cysteine is ligated to tRNA(Cys) by cysteinyl-tRNA synthetase in most organisms. However, in methanogenic archaea lacking cysteinyl-tRNA synthetase, O-phosphoserine is ligated to tRNA(Cys) by O-phosphoseryl-tRNA synthetase (SepRS), and the phosphoseryl-tRNA(Cys) is converted to cysteinyl-tRNA(Cys). In this study, we determined the crystal structure of the SepRS tetramer in complex with tRNA(Cys) and O-phosphoserine at 2.6-A resolution. The catalytic domain of SepRS recognizes the negatively charged side chain of O-phosphoserine at a noncanonical site, using the dipole moment of a conserved alpha-helix. The unique C-terminal domain specifically recognizes the anticodon GCA of tRNA(Cys). On the basis of the structure, we engineered SepRS to recognize tRNA(Cys) mutants with the anticodons UCA and CUA and clarified the anticodon recognition mechanism by crystallography. The mutant SepRS-tRNA pairs may be useful for translational incorporation of O-phosphoserine into proteins in response to the stop codons UGA and UAG.
Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea.,Fukunaga R, Yokoyama S Nat Struct Mol Biol. 2007 Apr;14(4):272-9. Epub 2007 Mar 11. PMID:17351629[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sauerwald A, Zhu W, Major TA, Roy H, Palioura S, Jahn D, Whitman WB, Yates JR 3rd, Ibba M, Soll D. RNA-dependent cysteine biosynthesis in archaea. Science. 2005 Mar 25;307(5717):1969-72. PMID:15790858 doi:http://dx.doi.org/10.1126/science.1108329
- ↑ Fukunaga R, Yokoyama S. Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Nat Struct Mol Biol. 2007 Apr;14(4):272-9. Epub 2007 Mar 11. PMID:17351629 doi:10.1038/nsmb1219
|
