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1bs2

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[[Image:1bs2.gif|left|200px]]
 
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==YEAST ARGINYL-TRNA SYNTHETASE==
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The line below this paragraph, containing "STRUCTURE_1bs2", creates the "Structure Box" on the page.
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<StructureSection load='1bs2' size='340' side='right'caption='[[1bs2]], [[Resolution|resolution]] 2.75&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'>[[1bs2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BS2 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]] 2.75&#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=ARG:ARGININE'>ARG</scene></td></tr>
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{{STRUCTURE_1bs2| PDB=1bs2 | 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=1bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bs2 OCA], [https://pdbe.org/1bs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bs2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bs2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYRC_YEAST SYRC_YEAST] Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (By similarity).[HAMAP-Rule:MF_00123]
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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/bs/1bs2_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=1bs2 ConSurf].
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<div style="clear:both"></div>
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'''YEAST ARGINYL-TRNA SYNTHETASE'''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of arginyl-tRNA synthetase (ArgRS) from Saccharomyces cerevisiae, a class I aminoacyl-tRNA synthetase (aaRS), with L-arginine bound to the active site has been solved at 2.75 A resolution and refined to a crystallographic R-factor of 19.7%. ArgRS is composed predominantly of alpha-helices and can be divided into five domains, including the class I-specific active site. The N-terminal domain shows striking similarity to some completely unrelated proteins and defines a module which should participate in specific tRNA recognition. The C-terminal domain, which is the putative anticodon-binding module, displays an all-alpha-helix fold highly similar to that of Escherichia coli methionyl-tRNA synthetase. While ArgRS requires tRNAArg for the first step of the aminoacylation reaction, the results show that its presence is not a prerequisite for L-arginine binding. All H-bond-forming capability of L-arginine is used by the protein for the specific recognition. The guanidinium group forms two salt bridge interactions with two acidic residues, and one H-bond with a tyrosine residue; these three residues are strictly conserved in all ArgRS sequences. This tyrosine is also conserved in other class I aaRS active sites but plays several functional roles. The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs.
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[[Category: Large Structures]]
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==About this Structure==
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1BS2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BS2 OCA].
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==Reference==
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L-arginine recognition by yeast arginyl-tRNA synthetase., Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D, EMBO J. 1998 Sep 15;17(18):5438-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9736621 9736621]
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[[Category: Arginine--tRNA ligase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Cavarelli J]]
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[[Category: Cavarelli, J.]]
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[[Category: Delagouute B]]
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[[Category: Delagouute, B.]]
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[[Category: Eriani G]]
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[[Category: Eriani, G.]]
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[[Category: Gangloff J]]
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[[Category: Gangloff, J.]]
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[[Category: Moras D]]
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[[Category: Moras, D.]]
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[[Category: Aminoacyl-trna synthetase]]
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[[Category: Ligase]]
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[[Category: Protein biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:53:15 2008''
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Current revision

YEAST ARGINYL-TRNA SYNTHETASE

PDB ID 1bs2

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