Solution structure and DNA binding of the catalytic domain of the large serine resolvase TnpX-Reference-Cited by-同舟云学术

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Solution structure and DNA binding of the catalytic domain of the large serine resolvase TnpX

Published:2015-02-26 Issue:5 Volume:28 Page:316-324
ISSN:0952-3499
Container-title:Journal of Molecular Recognition
language:en
Short-container-title:J. Mol. Recognit.

Author:

Headey Stephen J.¹,Sivakumaran Andrew²,Adams Vicki³,Lyras Dena³,Rood Julian I.³,Scanlon Martin J.¹,Wilce Matthew C. J.²

Affiliation:

1. Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences; Monash University; Parkville Victoria 3052 Australia

2. Department of Biochemistry and Molecular Biology; Clayton Victoria 3800 Australia

3. Department of Microbiology; Monash University; Clayton Victoria 3800 Australia

Publisher

Wiley

Subject

Molecular Biology,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/jmr.2446/fullpdf

Reference31 articles.

1. The clostridial mobilisable transposons;Adams;Cell. Mol. Life Sci.,2002

2. DNA binding properties of TnpX indicate that different synapses are formed in the excision and integration of the Tn4451 family;Adams;Mol. Microbiol.,2004

3. Two distinct regions of the large serine recombinase TnpX are required for DNA binding and biological function;Adams;Mol. Microbiol.,2006

4. The Program Xeasy for Computer-Supported Nmr Spectral-Analysis of Biological Macromolecules;Bartels;J. Biomol. NMR,1995

5. Integration and excision by the large serine recombinase phi Rv1 integrase;Bibb;Mol. Microbiol.,2005

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1. Antibiotic resistance plasmids and mobile genetic elements of Clostridium perfringens;Plasmid;2018-09

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