1bcm
BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNITBACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT
Structural highlights
Function[TRA_BPMU] This transposase is essential for integration, replication-transposition, and excision of Mu DNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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