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| | ==Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate== | | ==Crystal Structure of mammalian mitochondrial seryl-tRNA synthetase complexed with seryl-adenylate== |
| - | <StructureSection load='1wle' size='340' side='right' caption='[[1wle]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='1wle' size='340' side='right'caption='[[1wle]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wle]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WLE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wle]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SRP:SERYL+ADENYLATE'>SRP</scene></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]] 1.65Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SerRSmt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SRP:SERYL+ADENYLATE'>SRP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine--tRNA_ligase Serine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.11 6.1.1.11] </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=1wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wle OCA], [https://pdbe.org/1wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wle RCSB], [https://www.ebi.ac.uk/pdbsum/1wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wle ProSAT]</span></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=1wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wle OCA], [http://pdbe.org/1wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wle RCSB], [http://www.ebi.ac.uk/pdbsum/1wle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wle ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYSM_BOVIN SYSM_BOVIN]] Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).<ref>PMID:10764807</ref> | + | [https://www.uniprot.org/uniprot/SYSM_BOVIN SYSM_BOVIN] Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).<ref>PMID:10764807</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==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: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Serine--tRNA ligase]] | + | [[Category: Large Structures]] |
| - | [[Category: Chimnaronk, S]] | + | [[Category: Chimnaronk S]] |
| - | [[Category: Jeppesen, M G]] | + | [[Category: Jeppesen MG]] |
| - | [[Category: Nyborg, J]] | + | [[Category: Nyborg J]] |
| - | [[Category: Suzuki, T]] | + | [[Category: Suzuki T]] |
| - | [[Category: Watanabe, K]] | + | [[Category: Watanabe K]] |
| - | [[Category: Ligase]]
| + | |
| Structural highlights
Function
SYSM_BOVIN Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).[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
The secondary structures of metazoan mitochondrial (mt) tRNAs(Ser) deviate markedly from the paradigm of the canonical cloverleaf structure; particularly, tRNA(Ser)(GCU) corresponding to the AGY codon (Y=U and C) is highly truncated and intrinsically missing the entire dihydrouridine arm. None of the mt serine isoacceptors possesses the elongated variable arm, which is the universal landmark for recognition by seryl-tRNA synthetase (SerRS). Here, we report the crystal structure of mammalian mt SerRS from Bos taurus in complex with seryl adenylate at an atomic resolution of 1.65 A. Coupling structural information with a tRNA-docking model and the mutagenesis studies, we have unraveled the key elements that establish tRNA binding specificity, differ from all other known bacterial and eukaryotic systems, are the characteristic extensions in both extremities, as well as a few basic residues residing in the amino-terminal helical arm of mt SerRS. Our data further uncover an unprecedented mechanism of a dual-mode recognition employed to discriminate two distinct 'bizarre' mt tRNAs(Ser) by alternative combination of interaction sites.
Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria.,Chimnaronk S, Gravers Jeppesen M, Suzuki T, Nyborg J, Watanabe K EMBO J. 2005 Oct 5;24(19):3369-79. Epub 2005 Sep 15. PMID:16163389[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K. Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem. 2000 Jun 30;275(26):19913-20. PMID:10764807 doi:10.1074/jbc.M908473199
- ↑ Chimnaronk S, Gravers Jeppesen M, Suzuki T, Nyborg J, Watanabe K. Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria. EMBO J. 2005 Oct 5;24(19):3369-79. Epub 2005 Sep 15. PMID:16163389
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