2GM4

An activated, tetrameric gamma-delta resolvase: Hin chimaera bound to cleaved DNA

Summary for 2GM4

• Entry DOI: 10.2210/pdb2gm4/pdb
• Related: 1GDT 1ZR2 1ZR4 2GM5 2RSL
• Descriptor: 5'-D(*CP*AP*GP*TP*GP*TP*CP*CP*GP*AP*TP*AP*AP*TP*TP*TP*AP*TP*AP*AP*A)-3', 5'-D(*TP*TP*AP*TP*CP*GP*GP*AP*CP*AP*CP*TP*G)-3', Transposon gamma-delta resolvase (3 entities in total)
• Functional Keywords: gamma delta resolvase, protein dna complex, site specific recombination, recombination, dna
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 74388.94

Authors

Kamtekar, S.,Ho, R.S.,Li, W.,Steitz, T.A. (deposition date: 2006-04-05, release date: 2006-06-27, Last modification date: 2023-08-30)

Primary citation

Kamtekar, S.,Ho, R.S.,Cocco, M.J.,Li, W.,Wenwieser, S.V.,Boocock, M.R.,Grindley, N.D.,Steitz, T.A.
Implications of structures of synaptic tetramers of gamma delta resolvase for the mechanism of recombination.
Proc.Natl.Acad.Sci.Usa, 103:10642-10647, 2006

PubMed Abstract: The structures of two mutants of the site-specific recombinase, gammadelta resolvase, that form activated tetramers have been determined. One, at 3.5-A resolution, forms a synaptic intermediate of resolvase that is covalently linked to two cleaved DNAs, whereas the other is of an unliganded structure determined at 2.1-A resolution. Comparisons of the four known tetrameric resolvase structures show that the subunits interact through the formation of a common core of four helices. The N-terminal halves of these helices superimpose well on each other, whereas the orientations of their C termini are more variable. The catalytic domains of resolvase in the unliganded structure are arranged asymmetrically, demonstrating that their positions can move substantially while preserving the four-helix core that forms the tetramer. These results suggest that the precleavage synaptic tetramer of gammadelta resolvase, whose structure is not known, may be formed by a similar four-helix core, but differ in the relative orientations of its catalytic and DNA-binding domains.

PubMed: 16807292
DOI: 10.1073/pnas.0604062103

Experimental method

X-RAY DIFFRACTION (3.5 Å)