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1y42

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[[Image:1y42.gif|left|200px]]
 
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==Crystal structure of a C-terminally truncated CYT-18 protein==
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The line below this paragraph, containing "STRUCTURE_1y42", creates the "Structure Box" on the page.
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<StructureSection load='1y42' size='340' side='right'caption='[[1y42]], [[Resolution|resolution]] 1.95&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'>[[1y42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y42 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]] 1.95&#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=TYR:TYROSINE'>TYR</scene></td></tr>
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{{STRUCTURE_1y42| PDB=1y42 | 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=1y42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y42 OCA], [https://pdbe.org/1y42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y42 RCSB], [https://www.ebi.ac.uk/pdbsum/1y42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y42 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYYM_NEUCR SYYM_NEUCR] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by stabilizing the catalytically active structure of the intron.
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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/y4/1y42_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=1y42 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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We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.
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'''Crystal structure of a C-terminally truncated CYT-18 protein'''
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A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface.,Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM Mol Cell. 2005 Feb 4;17(3):417-28. PMID:15694342<ref>PMID:15694342</ref>
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==Overview==
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We determined a 1.95 A X-ray crystal structure of a C-terminally truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions in splicing group I introns. CYT-18's nucleotide binding fold and intermediate alpha-helical domains superimpose on those of bacterial TyrRSs, except for an N-terminal extension and two small insertions not found in nonsplicing bacterial enzymes. These additions surround the cyt-18-1 mutation site and are sites of suppressor mutations that restore splicing, but not synthetase activity. Highly constrained models based on directed hydroxyl radical cleavage assays show that the group I intron binds at a site formed in part by the three additions on the nucleotide binding fold surface opposite that which binds tRNATyr. Our results show how essential proteins can progressively evolve new functions.
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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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1Y42 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y42 OCA].
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</div>
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<div class="pdbe-citations 1y42" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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A tyrosyl-tRNA synthetase adapted to function in group I intron splicing by acquiring a new RNA binding surface., Paukstelis PJ, Coon R, Madabusi L, Nowakowski J, Monzingo A, Robertus J, Lambowitz AM, Mol Cell. 2005 Feb 4;17(3):417-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15694342 15694342]
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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>
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[[Category: Large Structures]]
[[Category: Neurospora crassa]]
[[Category: Neurospora crassa]]
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[[Category: Single protein]]
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[[Category: Coon R]]
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Lambowitz AM]]
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[[Category: Coon, R.]]
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[[Category: Madabusi L]]
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[[Category: Lambowitz, A M.]]
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[[Category: Monzingo A]]
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[[Category: Madabusi, L.]]
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[[Category: Nowakowski J]]
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[[Category: Monzingo, A.]]
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[[Category: Paukstelis PJ]]
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[[Category: Nowakowski, J.]]
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[[Category: Robertus J]]
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[[Category: Paukstelis, P J.]]
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[[Category: Robertus, J.]]
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[[Category: Cyt-18]]
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[[Category: Group i intron]]
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[[Category: Trna ligase]]
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[[Category: Tyrosyl trna synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:51:07 2008''
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Current revision

Crystal structure of a C-terminally truncated CYT-18 protein

PDB ID 1y42

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