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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[3cmq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CMQ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3cmq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CMQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FA5:ADENOSINE-5-[PHENYLALANINYL-PHOSPHATE]'>FA5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pys|1pys]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FA5:ADENOSINE-5-[PHENYLALANINYL-PHOSPHATE]'>FA5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FARS2, FARS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] </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=3cmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cmq OCA], [https://pdbe.org/3cmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cmq RCSB], [https://www.ebi.ac.uk/pdbsum/3cmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cmq ProSAT]</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=3cmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cmq OCA], [https://pdbe.org/3cmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cmq RCSB], [https://www.ebi.ac.uk/pdbsum/3cmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cmq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SYFM_HUMAN SYFM_HUMAN]] Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.<ref>PMID:19549855</ref>
| + | [https://www.uniprot.org/uniprot/SYFM_HUMAN SYFM_HUMAN] Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.<ref>PMID:19549855</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phenylalanine--tRNA ligase]]
| + | [[Category: Finarov I]] |
| - | [[Category: Finarov, I]] | + | [[Category: Kessler N]] |
| - | [[Category: Kessler, N]] | + | [[Category: Klipcan L]] |
| - | [[Category: Klipcan, L]] | + | [[Category: Levin IL]] |
| - | [[Category: Levin, I L]] | + | [[Category: Moor N]] |
| - | [[Category: Moor, N]] | + | [[Category: Safro M]] |
| - | [[Category: Safro, M]] | + | |
| - | [[Category: Aminoacyl-trna synthetase]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Classii aarss fold]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Rna recogntion]]
| + | |
| - | [[Category: Rrm domain]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| - | [[Category: Trna]]
| + | |
| Structural highlights
Function
SYFM_HUMAN Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.[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
All class II aminoacyl-tRNA synthetases (aaRSs) are known to be active as functional homodimers, homotetramers, or heterotetramers. However, multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase (PheRS) is also active. We herein report the structure, at 2.2 A resolution, of a human monomeric mitPheRS complexed with Phe-AMP. The smallest known aaRS, which is, in fact, 1/5 of a cytoplasmic analog, is a chimera of the catalytic module of the alpha and anticodon binding domain (ABD) of the bacterial beta subunit of (alphabeta)2 PheRS. We demonstrate that the ABD located at the C terminus of mitPheRS overlaps with the acceptor stem of phenylalanine transfer RNA (tRNAPhe) if the substrate is positioned in a manner similar to that seen in the binary Thermus thermophilus complex. Thus, formation of the PheRS-tRNAPhe complex in human mitochondria must be accompanied by considerable rearrangement (hinge-type rotation through approximately 160 degrees) of the ABD upon tRNA binding.
The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase.,Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M Structure. 2008 Jul;16(7):1095-104. PMID:18611382[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Klipcan L, Moor N, Kessler N, Safro MG. Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine. Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11045-8. Epub 2009 Jun 22. PMID:19549855
- ↑ Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M. The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase. Structure. 2008 Jul;16(7):1095-104. PMID:18611382 doi:10.1016/j.str.2008.03.020
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