1bs2

<StructureSection load='1bs2' size='340' side='right' caption='[[1bs2]], [[Resolution|resolution]] 2.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1bs2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BS2 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] </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=1bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bs2 OCA], [http://pdbe.org/1bs2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/1bs2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bs2 ProSAT]</span></td></tr>

[[http://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]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/1bs2_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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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== References ==

[[Category: Arginine--tRNA ligase]]

[[Category: Atcc 18824]]

[[Category: Cavarelli, J]]

[[Category: Delagouute, B]]

[[Category: Eriani, G]]

[[Category: Gangloff, J]]

[[Category: Moras, D]]

[[Category: Protein biosynthesis]]