1nyl

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[[Image:1nyl.jpg|left|200px]]
 
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==Unliganded glutaminyl-tRNA synthetase==
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The line below this paragraph, containing "STRUCTURE_1nyl", creates the "Structure Box" on the page.
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<StructureSection load='1nyl' size='340' side='right'caption='[[1nyl]], [[Resolution|resolution]] 2.60&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'>[[1nyl]] is a 1 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=1NYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NYL 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]] 2.6&#8491;</td></tr>
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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=1nyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyl OCA], [https://pdbe.org/1nyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nyl RCSB], [https://www.ebi.ac.uk/pdbsum/1nyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nyl ProSAT]</span></td></tr>
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{{STRUCTURE_1nyl| PDB=1nyl | SCENE= }}
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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/ny/1nyl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nyl 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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The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.
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'''Unliganded glutaminyl-tRNA synthetase'''
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tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase.,Sherlin LD, Perona JJ Structure. 2003 May;11(5):591-603. PMID:12737824<ref>PMID:12737824</ref>
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==Overview==
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The crystal structure of ligand-free E. coli glutaminyl-tRNA synthetase (GlnRS) at 2.4 A resolution shows that substrate binding is essential to construction of a catalytically proficient active site. tRNA binding generates structural changes throughout the enzyme, repositioning key active site peptides that bind glutamine and ATP. The structure gives insight into longstanding questions regarding the tRNA dependence of glutaminyl adenylate formation, the coupling of amino acid and tRNA selectivities, and the roles of specific pathways for transmission of tRNA binding signals to the active site. Comparative analysis of the unliganded and tRNA-bound structures shows, in detail, how flexibility is built into the enzyme architecture and suggests that the induced-fit transitions are a key underlying determinant of both amino acid and tRNA specificity.
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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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1NYL 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=1NYL OCA].
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</div>
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<div class="pdbe-citations 1nyl" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase., Sherlin LD, Perona JJ, Structure. 2003 May;11(5):591-603. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12737824 12737824]
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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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: Perona JP]]
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[[Category: Perona, J P.]]
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[[Category: Sherlin LD]]
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[[Category: Sherlin, L D.]]
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[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:08:37 2008''
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Current revision

Unliganded glutaminyl-tRNA synthetase

PDB ID 1nyl

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