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Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine...

Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3088605

Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine recombinase

About this item

Full title

Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine recombinase

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2011-05, Vol.108 (18), p.7419-7424

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Structural and topological data suggest that serine site-specific DNA recombinases exchange duplex DNAs by rigid-body relative rotation of the two halves of the synapse, mediated by a flat protein-protein interaction surface. We present evidence for this rotational motion for a simple serine recombinase, the Bxb1 phage integrase, from a single-DNA-...

Alternative Titles

Full title

Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine recombinase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3088605

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3088605

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1018436108

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