4r1j

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of Arc1p-C

Structural highlights

4r1j is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4]

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^[5]

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

References

↑ Deinert K, Fasiolo F, Hurt EC, Simos G. Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem. 2001 Feb 23;276(8):6000-8. PMID:11069915 doi:10.1074/jbc.M008682200
↑ Golinelli-Cohen MP, Mirande M. Arc1p is required for cytoplasmic confinement of synthetases and tRNA. Mol Cell Biochem. 2007 Jun;300(1-2):47-59. PMID:17131041 doi:10.1007/s11010-006-9367-4
↑ Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the EMBO J. 1996 Oct 1;15(19):5437-48 PMID:8895587
↑ Simos G, Sauer A, Fasiolo F, Hurt EC. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol Cell. 1998 Jan;1(2):235-42. PMID:9659920 doi:10.1016/s1097-2765(00)80024-6
↑ Giessen TW, Altegoer F, Nebel AJ, Steinbach RM, Bange G, Marahiel MA. A Synthetic Adenylation-Domain-Based tRNA-Aminoacylation Catalyst. Angew Chem Int Ed Engl. 2015 Feb 16;54(8):2492-6. doi: 10.1002/anie.201410047., Epub 2015 Jan 12. PMID:25583137 doi:http://dx.doi.org/10.1002/anie.201410047

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r1j"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Altegoer F | Bange G

@@ Line 1: / Line 1: @@
 ==Crystal structure of Arc1p-C==
-<StructureSection load='4r1j' size='340' side='right' caption='[[4r1j]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<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. 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>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+</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='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>
+<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 ==
-[[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.
+[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 ==
@@ Line 16: / Line 18: @@
 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: Altegoer, F]]
+[[Category: Large Structures]]
-[[Category: Bange, G]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Emap]]
+[[Category: Altegoer F]]
-[[Category: Rna binding protein]]
+[[Category: Bange G]]
-[[Category: Trna]]
-[[Category: Trna binding]]

4r1j

From Proteopedia

Current revision

Crystal structure of Arc1p-C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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