6f87: Difference between revisions
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<StructureSection load='6f87' size='340' side='right' caption='[[6f87]], [[Resolution|resolution]] 2.62Å' scene=''> | <StructureSection load='6f87' size='340' side='right' caption='[[6f87]], [[Resolution|resolution]] 2.62Å' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[6f87]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrab Pyrab]. 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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sua5, PYRAB15960, PAB1302 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272844 PYRAB])</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='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> | <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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: L-threonylcarbamoyladenylate synthase]] | [[Category: L-threonylcarbamoyladenylate synthase]] | ||
[[Category: Pyrab]] | |||
[[Category: Basta, T]] | [[Category: Basta, T]] | ||
[[Category: Collinet, B]] | [[Category: Collinet, B]] | ||
Latest revision as of 08:57, 27 June 2018
Crystal structure of P. abyssi Sua5 complexed with L-threonine and PPiCrystal structure of P. abyssi Sua5 complexed with L-threonine and PPi
Structural highlights
Function[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.[1] Publication Abstract from PubMedN6-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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