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| | <StructureSection load='3w1h' size='340' side='right'caption='[[3w1h]], [[Resolution|resolution]] 3.89Å' scene=''> | | <StructureSection load='3w1h' size='340' side='right'caption='[[3w1h]], [[Resolution|resolution]] 3.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w1h]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w1h]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1H FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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]] 3.893Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3w1i|3w1i]], [[3w1j|3w1j]], [[3w1k|3w1k]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">selA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.9.1.1 2.9.1.1] </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=3w1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1h OCA], [https://pdbe.org/3w1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1h RCSB], [https://www.ebi.ac.uk/pdbsum/3w1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1h 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=3w1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1h OCA], [https://pdbe.org/3w1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1h RCSB], [https://www.ebi.ac.uk/pdbsum/3w1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).
| + | [https://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Itoh, Y]] | + | [[Category: Itoh Y]] |
| - | [[Category: Sekine, S]] | + | [[Category: Sekine S]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Homodecamer]]
| + | |
| - | [[Category: Pentamer of dimer]]
| + | |
| - | [[Category: Selenium metabolism]]
| + | |
| - | [[Category: Selenocysteine synthesis]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
SELA_AQUAE Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).
Publication Abstract from PubMed
The 21st amino acid, selenocysteine (Sec), is synthesized on its cognate transfer RNA (tRNA(Sec)). In bacteria, SelA synthesizes Sec from Ser-tRNA(Sec), whereas in archaea and eukaryotes SepSecS forms Sec from phosphoserine (Sep) acylated to tRNA(Sec). We determined the crystal structures of Aquifex aeolicus SelA complexes, which revealed a ring-shaped homodecamer that binds 10 tRNA(Sec) molecules, each interacting with four SelA subunits. The SelA N-terminal domain binds the tRNA(Sec)-specific D-arm structure, thereby discriminating Ser-tRNA(Sec) from Ser-tRNA(Ser). A large cleft is created between two subunits and accommodates the 3'-terminal region of Ser-tRNA(Sec). The SelA structures together with in vivo and in vitro enzyme assays show decamerization to be essential for SelA function. SelA catalyzes pyridoxal 5'-phosphate-dependent Sec formation involving Arg residues nonhomologous to those in SepSecS. Different protein architecture and substrate coordination of the bacterial enzyme provide structural evidence for independent evolution of the two Sec synthesis systems present in nature.
Decameric SelA*tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation.,Itoh Y, Brocker MJ, Sekine S, Hammond G, Suetsugu S, Soll D, Yokoyama S Science. 2013 Apr 5;340(6128):75-8. doi: 10.1126/science.1229521. PMID:23559248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Itoh Y, Brocker MJ, Sekine S, Hammond G, Suetsugu S, Soll D, Yokoyama S. Decameric SelA*tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation. Science. 2013 Apr 5;340(6128):75-8. doi: 10.1126/science.1229521. PMID:23559248 doi:10.1126/science.1229521
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