Related Experiment Video
Updated: May 4, 2026

The MultiBac Protein Complex Production Platform at the EMBL
Published on: July 11, 2013
Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0540, USA.
Abstract:
The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4 A resolution. The first of two subdomains contains the active site and, despite very limited sequence homology, exhibits a striking similarity to the core domain of HIV-1 integrase, which carries out a similar set of biochemical reactions. It also exhibits more limited similarity to other nucleases, RNase H and RuvC. The second, a beta barrel, connects to the first subdomain through several contacts. Three independent determinations of the monomer structure from two crystal forms all show the active site held in a similar, apparently inactive configuration. The enzymatic activity of MuA is known to be activated by formation of a DNA-bound tetramer of the protein. We propose that the connections between the two subdomains may be involved in the cross-talk between the active site and the other domains of the transposase that controls the activity of the protein.
Insights
The crystal structure of bacteriophage Mu transposase (MuA) reveals a similarity to HIV-1 integrase. Its active site appears inactive in monomeric form, suggesting DNA binding activates MuA.
Area of Science:
- Structural Biology
- Molecular Biology
- Biochemistry
Background:
- Bacteriophage Mu transposase (MuA) is essential for viral DNA integration.
- Understanding MuA's structure is key to elucidating its catalytic mechanism.
- MuA shares functional similarities with other DNA-processing enzymes like HIV-1 integrase.
Purpose of the Study:
- To determine the high-resolution crystal structure of the MuA core domain.
- To compare the structural features of MuA with related enzymes.
- To investigate the structural basis for MuA's regulation and activation.
Main Methods:
- X-ray crystallography at 2.4 A resolution.
- Analysis of three independent monomer structures from two crystal forms.
- Comparative structural analysis with other nucleases.
Main Results:
- The crystal structure of the MuA core domain was elucidated.
- MuA's active site subdomain shows significant structural similarity to HIV-1 integrase.
- The active site was consistently observed in an apparently inactive conformation in the monomer.
- A beta-barrel subdomain connects to the active site subdomain.
Conclusions:
- MuA's structure shares conserved features with other integrases, suggesting a common evolutionary origin or functional adaptation.
- The inactive conformation of the active site in the monomer implies a regulatory mechanism.
- Interactions between subdomains may control MuA activity, potentially linking DNA binding to activation.
Related Concept Videos
Viral Structure
Intracellular Movement of Viruses and Bacteria
Mechanism of Conjugation
Viral Replication: Lytic Cycle
DNA Bacteriophages
Viruses with RNA Genomes

