Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Elizabeth J. Little"'
Autor:
Chad K Park, Hemant K Joshi, Alka Agrawal, M Imran Ghare, Elizabeth J Little, Pete W Dunten, Jurate Bitinaite, Nancy C Horton
Publikováno v:
PLoS Biology, Vol 8, Iss 12, p e1000554 (2010)
SgrAI is a type IIF restriction endonuclease that cuts an unusually long recognition sequence and exhibits allosteric self-modulation of cleavage activity and sequence specificity. Previous studies have shown that DNA bound dimers of SgrAI oligomeriz
Externí odkaz:
https://doaj.org/article/fc8be480579840c180cff46a54d26e20
Autor:
Charles W. Putnam, Elizabeth J. Little, Ted Weinert, Lisa Shanks, Rhett J. Michelson, P. Sundareshan, R. Gardner, Kara A. Nyberg, Anthony A. Admire
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 65:433-442
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55ead2591add4c1fa3aaceda3ba932f2
https://doi.org/10.1101/sqb.2000.65.433
https://doi.org/10.1101/sqb.2000.65.433
Publikováno v:
Journal of Molecular Evolution. 39:631-643
The evolutionary spread of 22 fibronectin type III (Fn3) sequences among a dozen bacterial enzymes has been traced by searching databases with the non-Fn3 parts of the enzyme sequences. Numerous homologues were found that lacked the Fn3 domains. In e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59c93ddff84cb8917918baf32100509f
https://doi.org/10.1007/bf00160409
https://doi.org/10.1007/bf00160409
SgrAI is a type II restriction endonuclease that cuts an unusually long recognition sequence and exhibits allosteric self-activation with expansion of DNA-sequence specificity. The three-dimensional crystal structures of SgrAI bound to cleaved primar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c75c5a89f5e46edff59c5bb4d325e8c
https://europepmc.org/articles/PMC3016018/
https://europepmc.org/articles/PMC3016018/
SummaryControl of replication, transcription, recombination and repair requires proteins capable of finding particular DNA sequences in a background of a large excess of nonspecific sequences. Such recognition can involve direct readout, with direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dd9ac549f1815432dbc53c3ea1c6291
https://europepmc.org/articles/PMC2637360/
https://europepmc.org/articles/PMC2637360/
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 65(Pt 4)
Uninterpretable electron-density maps were obtained using either MIRAS phases or MR phases in attempts to determine the structure of the type II restriction endonuclease SgrAI bound to DNA. While neither solution strategy was particularly promising (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::165e7cab0b38e0536bfd12984c0e04f5
https://pubmed.ncbi.nlm.nih.gov/19307723
https://pubmed.ncbi.nlm.nih.gov/19307723
Five new structures of the Q138F HincII enzyme bound to a total of three different DNA sequences and three different metal ions (Ca{sup 2+}, Mg{sup 2+}, and Mn{sup 2+}) are presented. While previous structures were produced from soaking Ca{sup 2+} in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a5e302d526a217025a26ebe09ae91bd
https://europepmc.org/articles/PMC2605692/
https://europepmc.org/articles/PMC2605692/
Autor:
Jurate Bitinaite, David M. Hough, Pete W. Dunten, V.M. Manohar, Elizabeth J. Little, Mark T. Gregory, Michael A. Dalton, Nancy C. Horton
Publikováno v:
Nucleic Acids Research
The three-dimensional X-ray crystal structure of the ‘rare cutting’ type II restriction endonuclease SgrAI bound to cognate DNA is presented. SgrAI forms a dimer bound to one duplex of DNA. Two Ca2+ bind in the enzyme active site, with one ion at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b90bfe35bdbd956785bee2a5fb32a8ed
https://pubmed.ncbi.nlm.nih.gov/18701646
https://pubmed.ncbi.nlm.nih.gov/18701646
Autor:
Elizabeth J. Little, Nancy C. Horton
Publikováno v:
Journal of molecular biology. 351(1)
The 2.1A crystal structure of the unliganded type II restriction endonuclease, HincII, is described. Although the asymmetric unit contains only a single monomer, crystal lattice contacts bring two monomers together to form a dimer very similar to tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::873db25afaeec10eeeb508c5b3ce54cb
https://pubmed.ncbi.nlm.nih.gov/15993893
https://pubmed.ncbi.nlm.nih.gov/15993893
Publikováno v:
Science. 274:1751-1753
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47cc9b941762bf6f1a7ca8b5c1bb8d68
https://doi.org/10.1126/science.274.5293.1751
https://doi.org/10.1126/science.274.5293.1751