1qtq

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[[Image:1qtq.gif|left|200px]]
 
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==GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG==
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The line below this paragraph, containing "STRUCTURE_1qtq", creates the "Structure Box" on the page.
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<StructureSection load='1qtq' size='340' side='right'caption='[[1qtq]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qtq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QTQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QSI:5-O-[N-(L-GLUTAMINYL)-SULFAMOYL]ADENOSINE'>QSI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1qtq| PDB=1qtq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtq OCA], [https://pdbe.org/1qtq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qtq RCSB], [https://www.ebi.ac.uk/pdbsum/1qtq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qtq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYQ_ECOLI SYQ_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/1qtq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qtq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Aminoacyl-tRNA synthetases covalently link a specific amino acid to the correct tRNA. The fidelity of this reaction is essential for accurate protein synthesis. Each synthetase has a specific molecular mechanism to distinguish the correct pair of substrates from the pool of amino acids and isologous tRNA molecules. In the case of glutaminyl-tRNA synthetase (GlnRS) the prior binding of tRNA is required for activation of glutamine by ATP. A complete understanding of amino acid specificity in GlnRS requires the determination of the structure of the synthetase with both tRNA and substrates bound. RESULTS: A stable glutaminly-adenylate analog, which inhibits GlnRS with a Ki of 1.32 microM, was synthesized and cocrystallized with GlnRS and tRNA2Gln. The crystal structure of this ternary complex has been refined at 2.4 A resolution and shows the interactions made between glutamine and its binding site. CONCLUSIONS: To select against glutamic acid or glutamate, both hydrogen atoms of the nitrogen of the glutamine sidechain are recognized. The hydroxyl group of Tyr211 and a water molecule are responsible for this recognition; both are obligate hydrogen-bond acceptors due to a network of interacting sidechains and water molecules. The prior binding of tRNAGln that is required for amino acid activation may result from the terminal nucleotide, A76, packing against and orienting Tyr211, which forms part of the amino acid binding site.
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'''GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG'''
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How glutaminyl-tRNA synthetase selects glutamine.,Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA Structure. 1998 Apr 15;6(4):439-49. PMID:9562563<ref>PMID:9562563</ref>
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==Overview==
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BACKGROUND: Aminoacyl-tRNA synthetases covalently link a specific amino acid to the correct tRNA. The fidelity of this reaction is essential for accurate protein synthesis. Each synthetase has a specific molecular mechanism to distinguish the correct pair of substrates from the pool of amino acids and isologous tRNA molecules. In the case of glutaminyl-tRNA synthetase (GlnRS) the prior binding of tRNA is required for activation of glutamine by ATP. A complete understanding of amino acid specificity in GlnRS requires the determination of the structure of the synthetase with both tRNA and substrates bound. RESULTS: A stable glutaminly-adenylate analog, which inhibits GlnRS with a Ki of 1.32 microM, was synthesized and cocrystallized with GlnRS and tRNA2Gln. The crystal structure of this ternary complex has been refined at 2.4 A resolution and shows the interactions made between glutamine and its binding site. CONCLUSIONS: To select against glutamic acid or glutamate, both hydrogen atoms of the nitrogen of the glutamine sidechain are recognized. The hydroxyl group of Tyr211 and a water molecule are responsible for this recognition; both are obligate hydrogen-bond acceptors due to a network of interacting sidechains and water molecules. The prior binding of tRNAGln that is required for amino acid activation may result from the terminal nucleotide, A76, packing against and orienting Tyr211, which forms part of the amino acid binding site.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1QTQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTQ OCA].
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</div>
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<div class="pdbe-citations 1qtq" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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How glutaminyl-tRNA synthetase selects glutamine., Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA, Structure. 1998 Apr 15;6(4):439-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9562563 9562563]
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glutamine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Beijer B]]
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[[Category: Beijer, B.]]
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[[Category: Rath VL]]
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[[Category: Rath, V L.]]
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[[Category: Silvian LF]]
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[[Category: Silvian, L F.]]
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[[Category: Sproat BS]]
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[[Category: Sproat, B S.]]
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[[Category: Steitz TA]]
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[[Category: Steitz, T A.]]
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[[Category: Complex]]
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[[Category: E. coli]]
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[[Category: Glutamine]]
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[[Category: Trna synthetase]]
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[[Category: Trnagln]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:41:42 2008''
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Current revision

GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH TRNA AND AN AMINO ACID ANALOG

PDB ID 1qtq

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