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{{STRUCTURE_3w1h|  PDB=3w1h | SCENE= }}
==Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicus==
===Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicus===
<StructureSection load='3w1h' size='340' side='right' caption='[[3w1h]], [[Resolution|resolution]] 3.89&Aring;' scene=''>
{{ABSTRACT_PUBMED_23559248}}
== Structural highlights ==
<table><tr><td colspan='2'>[[3w1h]] is a 5 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w1i|3w1i]], [[3w1j|3w1j]], [[3w1k|3w1k]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">selA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 Aquifex aeolicus VF5])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-seryl-tRNA(Sec)_selenium_transferase L-seryl-tRNA(Sec) selenium transferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3w1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w1h RCSB], [http://www.ebi.ac.uk/pdbsum/3w1h PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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;">
== 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.


==Function==
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<ref>PMID:23559248</ref>
[[http://www.uniprot.org/uniprot/SELA_AQUAE SELA_AQUAE]] Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis (By similarity).  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[3w1h]] is a 5 chain structure with sequence from [http://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].
</div>


==Reference==
==See Also==
<ref group="xtra">PMID:023559248</ref><references group="xtra"/><references/>
*[[Selenocysteine synthase|Selenocysteine synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus vf5]]
[[Category: Aquifex aeolicus vf5]]
[[Category: Itoh, Y.]]
[[Category: Itoh, Y]]
[[Category: Sekine, S.]]
[[Category: Sekine, S]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S]]
[[Category: Homodecamer]]
[[Category: Homodecamer]]
[[Category: Pentamer of dimer]]
[[Category: Pentamer of dimer]]

Revision as of 23:27, 25 December 2014

Crystal structure of the selenocysteine synthase SelA from Aquifex aeolicusCrystal structure of the selenocysteine synthase SelA from Aquifex aeolicus

Structural highlights

3w1h is a 5 chain structure with sequence from Aquifex aeolicus vf5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:selA (Aquifex aeolicus VF5)
Activity:L-seryl-tRNA(Sec) selenium transferase, with EC number 2.9.1.1
Resources:FirstGlance, OCA, RCSB, PDBsum

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

  1. ↑ 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

3w1h, resolution 3.89Å

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