4r1j: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 4r1j~~ is ~~ON HOLD~~

==Crystal structure of Arc1p-C==

== Structural highlights ==

<table><tr><td colspan='2'>[[4r1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4R1J FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1j OCA], [https://pdbe.org/4r1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r1j RCSB], [https://www.ebi.ac.uk/pdbsum/4r1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r1j ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/ARC1_YEAST ARC1_YEAST] Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.<ref>PMID:11069915</ref> <ref>PMID:17131041</ref> <ref>PMID:8895587</ref> <ref>PMID:9659920</ref>

== 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.

~~Authors:~~ Altegoer, F., Bange, G.

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>

~~Description: Crystal structure~~ of ~~Arc1p~~-C

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Saccharomyces cerevisiae S288C]]

[[Category: Altegoer F]]

[[Category: Bange G]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4r1j is ON HOLD
+==Crystal structure of Arc1p-C==
+<StructureSection load='4r1j' size='340' side='right'caption='[[4r1j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4r1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4R1J FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1j OCA], [https://pdbe.org/4r1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r1j RCSB], [https://www.ebi.ac.uk/pdbsum/4r1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r1j ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARC1_YEAST ARC1_YEAST] Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.<ref>PMID:11069915</ref> <ref>PMID:17131041</ref> <ref>PMID:8895587</ref> <ref>PMID:9659920</ref>
+<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.
-Authors: Altegoer, F., Bange, G.
+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>
-Description: Crystal structure of Arc1p-C
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4r1j" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae S288C]]
+[[Category: Altegoer F]]
+[[Category: Bange G]]