1tky

From Proteopedia

(Difference between revisions)

Revision as of 11:54, 24 December 2020

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine

Structural highlights

1tky is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1qf6, 1tje, 1tke, 1tkg
Gene:	THRS, B1719, C2116, SF1512, S1630 ("Bacillus coli" Migula 1895)
Activity:	Threonine--tRNA ligase, with EC number 6.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SYT_ECOLI] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]

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

The fidelity of aminoacylation of tRNA(Thr) by the threonyl-tRNA synthetase (ThrRS) requires the discrimination of the cognate substrate threonine from the noncognate serine. Misacylation by serine is corrected in a proofreading or editing step. An editing site has been located 39 A away from the aminoacylation site. We report the crystal structures of this editing domain in its apo form and in complex with the serine product, and with two nonhydrolyzable analogs of potential substrates: the terminal tRNA adenosine charged with serine, and seryl adenylate. The structures show how serine is recognized, and threonine rejected, and provide the structural basis for the editing mechanism, a water-mediated hydrolysis of the mischarged tRNA. When the adenylate analog binds in the editing site, a phosphate oxygen takes the place of one of the catalytic water molecules, thereby blocking the reaction. This rules out a correction mechanism that would occur before the binding of the amino acid on the tRNA.

Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution.,Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D Mol Cell. 2004 Nov 5;16(3):375-86. PMID:15525511^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D. Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution. Mol Cell. 2004 Nov 5;16(3):375-86. PMID:15525511 doi:http://dx.doi.org/10.1016/j.molcel.2004.10.002

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tky"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine==
-<StructureSection load='1tky' size='340' side='right' caption='[[1tky]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
+<StructureSection load='1tky' size='340' side='right'caption='[[1tky]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tky]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TKY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tky]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TKY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qf6|1qf6]], [[1tje|1tje]], [[1tke|1tke]], [[1tkg|1tkg]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qf6|1qf6]], [[1tje|1tje]], [[1tke|1tke]], [[1tkg|1tkg]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THRS, B1719, C2116, SF1512, S1630 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </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=1tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tky OCA], [http://pdbe.org/1tky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tky RCSB], [http://www.ebi.ac.uk/pdbsum/1tky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tky ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tky OCA], [http://pdbe.org/1tky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tky RCSB], [http://www.ebi.ac.uk/pdbsum/1tky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tky ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 ==See Also==
-*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 39: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Threonine--tRNA ligase]]
 [[Category: Bey, G]]

1tky

From Proteopedia

Revision as of 11:54, 24 December 2020

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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