4dg7: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dg7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DG7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4dg7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DG7 FirstGlance]. <br> | ||
</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=4dg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dg7 OCA], [https://pdbe.org/4dg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dg7 RCSB], [https://www.ebi.ac.uk/pdbsum/4dg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dg7 ProSAT]</span></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]] 4.195Å</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=4dg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dg7 OCA], [https://pdbe.org/4dg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dg7 RCSB], [https://www.ebi.ac.uk/pdbsum/4dg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dg7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q7JVK6_DROME Q7JVK6_DROME] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 16:43, 8 November 2023
Low resolution structure of Drosophila TranslinLow resolution structure of Drosophila Translin
Structural highlights
FunctionPublication Abstract from PubMedCrystals of native Drosophila melanogaster translin diffracted to 7 A resolution. Reductive methylation of the protein improved crystal quality. The native and methylated proteins showed similar profiles in size-exclusion chromatography analyses but the methylated protein displayed reduced DNA-binding activity. Crystals of the methylated protein diffracted to 4.2 A resolution at BM14 of the ESRF synchrotron. Crystals with 49% solvent content belonged to monoclinic space group P21 with eight protomers in the asymmetric unit. Only 2% of low-resolution structures with similar low percentage solvent content were found in the PDB. The crystal structure, solved by molecular replacement method, refined to R work (R free) of 0.24 (0.29) with excellent stereochemistry. The crystal structure clearly shows that drosophila protein exists as an octamer, and not as a decamer as expected from gel-filtration elution profiles. The similar octameric quaternary fold in translin orthologs and in translin-TRAX complexes suggests an up-down dimer as the basic structural subunit of translin-like proteins. The drosophila oligomer displays asymmetric assembly and increased radius of gyration that accounts for the observed differences between the elution profiles of human and drosophila proteins on gel-filtration columns. This study demonstrates clearly that low-resolution X-ray structure can be useful in understanding complex biological oligomers. Low-resolution structure of Drosophila translin.,Kumar V, Gupta GD FEBS Open Bio. 2012 Mar 15;2:37-46. doi: 10.1016/j.fob.2012.03.001. Print 2012. PMID:23650579[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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