3i7f
From Proteopedia
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<StructureSection load='3i7f' size='340' side='right'caption='[[3i7f]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3i7f' size='340' side='right'caption='[[3i7f]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3i7f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3i7f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I7F FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i7f OCA], [https://pdbe.org/3i7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i7f RCSB], [https://www.ebi.ac.uk/pdbsum/3i7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i7f ProSAT]</span></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=3i7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i7f OCA], [https://pdbe.org/3i7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i7f RCSB], [https://www.ebi.ac.uk/pdbsum/3i7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i7f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C4LZN0_ENTH1 C4LZN0_ENTH1] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3i7f ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3i7f ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of the aspartyl-tRNA synthetase from the eukaryotic parasite Entamoeba histolytica has been determined at 2.8Aresolution. Relative to homologous sequences, the E. histolytica protein contains a 43-residue insertion between the N-terminal anticodon binding domain and the C-terminal catalytic domain. The present structure reveals that this insertion extends an arm of the hinge region that has previously been shown to mediate interaction of aspartyl-tRNA synthetase with the cognate tRNA D-stem. Modeling indicates that this Entamoeba-specific insertion is likely to increase the interaction surface with the cognate tRNA(Asp). In doing so it may substitute functionally for an RNA-binding motif located in N-terminal extensions found in AspRS sequences from lower eukaryotes but absent in Entamoeba. The E. histolytica AspRS structure shows a well-ordered N-terminus that contributes to the AspRS dimer interface. | ||
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| - | Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica.,Merritt EA, Arakaki TL, Larson ET, Kelley A, Mueller N, Napuli AJ, Zhang L, Deditta G, Luft J, Verlinde CL, Fan E, Zucker F, Buckner FS, Van Voorhis WC, Hol WG Mol Biochem Parasitol. 2010 Feb;169(2):95-100. Epub 2009 Oct 27. PMID:19874856<ref>PMID:19874856</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3i7f" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Entamoeba histolytica]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arakaki | + | [[Category: Arakaki T]] |
| - | + | [[Category: Merritt EA]] | |
| - | [[Category: Merritt | + | |
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Current revision
Aspartyl tRNA synthetase from Entamoeba histolytica
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