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The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution

Sanderson, MR and Freemont, PS and Rice, PA and Goldman, A and Hatfull, GF and Grindley, NDF and Steitz, TA (1990) The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell, 63 (6). 1323 - 1329. ISSN 0092-8674

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Abstract

The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase has been determined at 2.7 Å resolution. Its first 120 amino acids form a central five-stranded, β-pleated sheet surrounded by five α helices. In one of the four dyad-related dimers, the two active site Ser-10 residues are 19 Å apart, perhaps close enough to contact and become covalently linked to the DNA at the recombination site. This dimer also forms the only closely packed tetramer found in the crystal. The subunit interface at a second dyad-related dimer is more extensive and more highly conserved among the homologous recombinases; however, its active site Ser-10 residues are more than 30 Å apart. Side chains, identified by mutations that eliminate catalysis but not DNA binding, are located on the subunit surface near the active site serine and at the interface between a third dyad-related pair of subunits of the tetramer. © 1990.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Sanderson, MR
Freemont, PS
Rice, PA
Goldman, A
Hatfull, GFgfh@pitt.eduGFH
Grindley, NDF
Steitz, TA
Date: 21 December 1990
Date Type: Publication
Journal or Publication Title: Cell
Volume: 63
Number: 6
Page Range: 1323 - 1329
DOI or Unique Handle: 10.1016/0092-8674(90)90427-g
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0092-8674
MeSH Headings: Binding Sites; Crystallization; DNA--metabolism; Macromolecular Substances; Models, Molecular; Mutagenesis; Nucleotidyltransferases--chemistry; Nucleotidyltransferases--genetics; Nucleotidyltransferases--metabolism; Protein Binding; Protein Conformation; Transposases; X-Ray Diffraction
PubMed ID: 2175678
Date Deposited: 12 Mar 2013 19:31
Last Modified: 02 Feb 2019 15:57
URI: http://d-scholarship.pitt.edu/id/eprint/17653

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