1BCM
BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT
Summary for 1BCM
| Entry DOI | 10.2210/pdb1bcm/pdb |
| Descriptor | BACTERIOPHAGE MU TRANSPOSASE (1 entity in total) |
| Functional Keywords | polynucleotidyl transferase, dna binding, endonuclease, integrase, transposase |
| Biological source | Enterobacteria phage Mu |
| Total number of polymer chains | 2 |
| Total formula weight | 73776.16 |
| Authors | Rice, P.A.,Mizuuchi, K. (deposition date: 1995-05-26, release date: 1995-10-15, Last modification date: 2024-02-07) |
| Primary citation | Rice, P.,Mizuuchi, K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell(Cambridge,Mass.), 82:209-220, 1995 Cited by PubMed 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. PubMed: 7628012DOI: 10.1016/0092-8674(95)90308-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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