6ipa
From Proteopedia
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<StructureSection load='6ipa' size='340' side='right'caption='[[6ipa]], [[Resolution|resolution]] 2.47Å' scene=''> | <StructureSection load='6ipa' size='340' side='right'caption='[[6ipa]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ipa]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IPA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ipa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemamoeba_vivax Haemamoeba vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IPA FirstGlance]. <br> |
</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=6ipa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ipa OCA], [http://pdbe.org/6ipa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ipa RCSB], [http://www.ebi.ac.uk/pdbsum/6ipa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ipa ProSAT]</span></td></tr> | </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=6ipa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ipa OCA], [http://pdbe.org/6ipa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ipa RCSB], [http://www.ebi.ac.uk/pdbsum/6ipa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ipa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Scaffold modules known as aminoacyl-tRNA synthetase (aaRS)-interacting multifunctional proteins (AIMPs), such as AIMP1/p43, AIMP2/p38 and AIMP3/p18, are important in driving the assembly of multi-aaRS (MARS) complexes in eukaryotes. Often, AIMPs contain an N-terminal glutathione S-transferase (GST)-like domain and a C-terminal OB-fold tRNA-binding domain. Recently, the apicomplexan-specific Plasmodium falciparum p43 protein (Pfp43) has been annotated as an AIMP and its tRNA binding, tRNA import and membrane association have been characterized. The crystal structures of both the N- and C-terminal domains of the Plasmodium vivax p43 protein (Pvp43), which is an ortholog of Pfp43, have been resolved. Analyses reveal the overall oligomeric structure of Pvp43 and highlight several notable features that show Pvp43 to be a soluble, cytosolic protein. The dimeric assembly of the N-terminal GST-like domain of Pvp43 differs significantly from canonical GST dimers, and it is tied to the C-terminal tRNA-binding domain via a linker region. This work therefore establishes a framework for dissecting the additional roles of p43 orthologs in eukaryotic multi-protein MARS complexes. | ||
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| + | Crystal structures of the two domains that constitute the Plasmodium vivax p43 protein.,Gupta S, Chhibber-Goel J, Sharma M, Parvez S, Harlos K, Sharma A, Yogavel M Acta Crystallogr D Struct Biol. 2020 Feb 1;76(Pt 2):135-146. doi:, 10.1107/S2059798319016413. Epub 2020 Jan 30. PMID:32038044<ref>PMID:32038044</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ipa" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Haemamoeba vivax]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gupta, S]] | [[Category: Gupta, S]] | ||
Revision as of 07:51, 11 March 2020
C-terminal EMAP II-like domain of p43 refined against twinned data
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