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4r1j
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of Arc1p-C== |
| + | <StructureSection load='4r1j' size='340' side='right' caption='[[4r1j]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </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> | ||
| + | <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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Altegoer, F]] | ||
[[Category: Bange, G]] | [[Category: Bange, G]] | ||
| - | [[Category: | + | [[Category: Emap]] |
| + | [[Category: Rna binding protein]] | ||
| + | [[Category: Trna]] | ||
| + | [[Category: Trna binding]] | ||
Revision as of 12:57, 18 February 2015
Crystal structure of Arc1p-C
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Categories: Altegoer, F | Bange, G | Emap | Rna binding protein | Trna | Trna binding
