1bcm | pdb_00001bcm
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BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT
Overview
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.
About this Structure
1BCM is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration., Rice P, Mizuuchi K, Cell. 1995 Jul 28;82(2):209-20. PMID:7628012
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