6DGC

Crystal structure of the C-terminal catalytic domain of ISC1926 TnpA, an IS607-like serine recombinase

Summary for 6DGC

• Entry DOI: 10.2210/pdb6dgc/pdb
• Descriptor: ISC1926 TnpA C-terminal catalytic domain (1 entity in total)
• Functional Keywords: is607-like serine recombinase, hydrolase
• Biological source: Sulfolobus sp. L00 11
• Total number of polymer chains: 4
• Total formula weight: 66653.32

Authors

Hancock, S.P.,Kumar, P.,Cascio, D.,Johnson, R.C. (deposition date: 2018-05-17, release date: 2018-07-18, Last modification date: 2023-10-11)

Primary citation

Chen, W.,Mandali, S.,Hancock, S.P.,Kumar, P.,Collazo, M.,Cascio, D.,Johnson, R.C.
Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition.
Elife, 7:-, 2018

PubMed Abstract: IS-family transposons are unusual because they do not have terminal inverted repeats or generate target site duplications. They encode two protein-coding genes, but only is required for transposition. Our X-ray structures confirm that TnpA is a member of the serine recombinase (SR) family, but the chemically-inactive quaternary structure of the dimer, along with the N-terminal location of the DNA binding domain, are different from other SRs. TnpA dimers from IS cooperatively associate with multiple subterminal repeats, which together with additional nonspecific binding, form a nucleoprotein filament on one transposon end that efficiently captures a second unbound end to generate the paired-end complex (PEC). Formation of the PEC does not require a change in the dimeric structure of the catalytic domain, but remodeling of the C-terminal α-helical region is involved. We posit that the PEC recruits a chemically-active conformer of TnpA to the transposon end to initiate DNA chemistry.

PubMed: 30289389
DOI: 10.7554/eLife.39611

Experimental method

X-RAY DIFFRACTION (2.92 Å)