Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad
- 24 January 2007
- journal article
- Published by Springer Nature in The EMBO Journal
- Vol. 26 (2) , 613-622
- https://doi.org/10.1038/sj.emboj.7601497
Abstract
EMBO Press is an editorially independent publishing platform for the development of EMBO scientific publications.Keywords
This publication has 46 references indexed in Scilit:
- Structural basis for DNA recognition and processing by UvrBNature Structural & Molecular Biology, 2006
- Tn 5 Transposase Active Site MutantsJournal of Biological Chemistry, 2002
- Two-metal active site binding of a Tn5 transposase synaptic complexNature Structural & Molecular Biology, 2002
- Single Active Site Catalysis of the Successive Phosphoryl Transfer Steps by DNA TransposasesCell, 2000
- MOLREP: an Automated Program for Molecular ReplacementJournal of Applied Crystallography, 1997
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- The C-terminal Region of the UvrB Protein of Escherichia coli Contains an Important Determinant for UvrC Binding to the Preincision Complex but Not the Catalytic Site for 3′-IncisionJournal of Biological Chemistry, 1995
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991