4dg7 | pdb_00004dg7
Low 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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