6f87: Difference between revisions
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==Crystal structure of P. abyssi Sua5 complexed with L-threonine and PPi== | |||
<StructureSection load='6f87' size='340' side='right' caption='[[6f87]], [[Resolution|resolution]] 2.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f87]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F87 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-threonylcarbamoyladenylate_synthase L-threonylcarbamoyladenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.87 2.7.7.87] </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=6f87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f87 OCA], [http://pdbe.org/6f87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f87 RCSB], [http://www.ebi.ac.uk/pdbsum/6f87 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f87 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SUA5_PYRAB SUA5_PYRAB]] Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Likely catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Does not bind tRNA.<ref>PMID:23258706</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N6-threonyl-carbamoyl adenosine (t6A) is a universal tRNA modification found at position 37, next to the anticodon, in almost all tRNAs decoding ANN codons (where N = A, U, G or C). t6A stabilizes the codon-anticodon interaction and hence promotes translation fidelity. The first step of the biosynthesis of t6A, the production of threonyl-carbamoyl adenylate (TC-AMP), is catalyzed by the Sua5/TsaC family of enzymes. While TsaC is a single domain protein, Sua5 enzymes are composed of the TsaC-like domain, a linker and an extra domain called SUA5 of unknown function. In the present study, we report structure-function analysis of Pyrococcus abyssi Sua5 (Pa-Sua5). Crystallographic data revealed binding sites for bicarbonate substrate and pyrophosphate product. The linker of Pa-Sua5 forms a loop structure that folds into the active site gorge and closes it. Using structure-guided mutational analysis we established that the conserved sequence motifs in the linker and the domain-domain interface are essential for the function of Pa-Sua5. We propose that the linker participates actively in the biosynthesis of TC-AMP by binding to ATP/PPi and by stabilizing the N-carboxy-L-threonine intermediate. Hence, TsaC orthologs which lack such a linker and SUA5 domain use different mechanism for TC-AMP synthesis. | |||
Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.,Pichard-Kostuch A, Zhang W, Liger D, Daugeron MC, Letoquart J, Li de la Sierra-Gallay I, Forterre P, Collinet B, van Tilbeurgh H, Basta T RNA. 2018 Apr 12. pii: rna.066092.118. doi: 10.1261/rna.066092.118. PMID:29650678<ref>PMID:29650678</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6f87" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: L-threonylcarbamoyladenylate synthase]] | |||
[[Category: Basta, T]] | |||
[[Category: Collinet, B]] | |||
[[Category: Daugeron, M C]] | |||
[[Category: Forterre, P]] | |||
[[Category: Letoquart, J]] | |||
[[Category: Liger, D]] | |||
[[Category: Pichard-Kostuch, A]] | |||
[[Category: Sierra-Gallay, I Li de la]] | |||
[[Category: Tilbeurgh, H van]] | |||
[[Category: Zhang, W]] | |||
[[Category: Nucleotidyltransferase]] | |||
[[Category: Threonylcarbamoylation]] | |||
[[Category: Transferase]] | |||
[[Category: Trna modification]] | |||