4r1j

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'''Unreleased structure'''
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==Crystal structure of Arc1p-C==
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<StructureSection load='4r1j' size='340' side='right' caption='[[4r1j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4r1j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R1J FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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=4r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r1j RCSB], [http://www.ebi.ac.uk/pdbsum/4r1j PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/G4P1_YEAST G4P1_YEAST]] Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The incorporation of non-proteinogenic amino acids represents a major challenge for the creation of functionalized proteins. The ribosomal pathway is limited to the 20-22 proteinogenic amino acids while nonribosomal peptide synthetases (NRPSs) are able to select from hundreds of different monomers. Introduced herein is a fusion-protein-based design for synthetic tRNA-aminoacylation catalysts based on combining NRPS adenylation domains and a small eukaryotic tRNA-binding domain (Arc1p-C). Using rational design, guided by structural insights and molecular modeling, the adenylation domain PheA was fused with Arc1p-C using flexible linkers and achieved tRNA-aminoacylation with both proteinogenic and non-proteinogenic amino acids. The resulting aminoacyl-tRNAs were functionally validated and the catalysts showed broad substrate specificity towards the acceptor tRNA. Our strategy shows how functional tRNA-aminoacylation catalysts can be created for bridging the ribosomal and nonribosomal worlds. This opens up new avenues for the aminoacylation of tRNAs with functional non-proteinogenic amino acids.
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The entry 4r1j is ON HOLD until Paper Publication
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A Synthetic Adenylation-Domain-Based tRNA-Aminoacylation Catalyst.,Giessen TW, Altegoer F, Nebel AJ, Steinbach RM, Bange G, Marahiel MA Angew Chem Int Ed Engl. 2015 Feb 16;54(8):2492-6. doi: 10.1002/anie.201410047., Epub 2015 Jan 12. PMID:25583137<ref>PMID:25583137</ref>
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Authors: Altegoer, F., Bange, G.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Crystal structure of Arc1p-C
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Altegoer, F]]
[[Category: Bange, G]]
[[Category: Bange, G]]
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[[Category: Altegoer, F]]
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[[Category: Emap]]
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[[Category: Rna binding protein]]
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[[Category: Trna]]
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[[Category: Trna binding]]

Revision as of 12:57, 18 February 2015

Crystal structure of Arc1p-C

4r1j, resolution 1.40Å

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