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Kumar V, Gupta GD. Low-resolution structure of Drosophila translin. FEBS Open Bio. 2012;2:37-46doi: 10.1016/j.fob.2012.03.001.
Kumar, V., & Gupta, G. D. (2012). Low-resolution structure of Drosophila translin. FEBS open bio, 237-46. https://doi.org/10.1016/j.fob.2012.03.001
Kumar, Vinay, and Gupta, Gagan D. "Low-resolution structure of Drosophila translin." FEBS open bio vol. 2 (2012): 37-46. doi: https://doi.org/10.1016/j.fob.2012.03.001
Kumar V, Gupta GD. Low-resolution structure of Drosophila translin. FEBS Open Bio. 2012 Mar 15;2:37-46. doi: 10.1016/j.fob.2012.03.001. Print 2012. PMID: 23650579; PMCID: PMC3642112.
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FEBS Open Bio. 2012 Mar 15;2:37-46. doi: 10.1016/j.fob.2012.03.001. Print 2012.

Low-resolution structure of Drosophila translin.

FEBS open bio

Vinay Kumar, Gagan D Gupta

Affiliations

  1. High Pressure & Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Mumbai 400085, India.

PMID: 23650579 PMCID: PMC3642112 DOI: 10.1016/j.fob.2012.03.001

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.

Keywords: Crystal structure; Drosophila melanogaster translin; Low-resolution structure refinement; Oligomeric status; Reductive methylation

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