4DG7

Low resolution structure of Drosophila Translin

Summary for 4DG7

• Entry DOI: 10.2210/pdb4dg7/pdb
• Related: 1J1J 1kEY 2QRX 2QVA 3AXJ 3RIU
• Descriptor: GM27569p (1 entity in total)
• Functional Keywords: translin-like fold, ssdna/rna binding, reductive methylation, dimethylamino-borane, formaldehyde, dna binding protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 8
• Total formula weight: 233833.77

Authors

Kumar, V.,Gupta, G.D. (deposition date: 2012-01-25, release date: 2012-06-06, Last modification date: 2023-11-29)

Primary citation

Kumar, V.,Gupta, G.D.
Low-resolution structure of Drosophila translin
FEBS Open Bio, 2:37-46, 2012

PubMed Abstract: Crystals of native Drosophila melanogaster translin diffracted to 7 Å 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 Å 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.

PubMed: 23650579
DOI: 10.1016/j.fob.2012.03.001

Experimental method

X-RAY DIFFRACTION (4.195 Å)