PDBsum entry 1bcm

Transposase

PDB id: 1bcm

Contents

Protein chains

304 a.a. *

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: Structure of the bacteriophage mu transposase core: a common structural motif for DNA transposition and retroviral integration.
• Authors: P.Rice, K.Mizuuchi.
• Ref.: Cell, 1995, 82, 209-220. [DOI no: 10.1016/0092-8674(95)90308-9]
• PubMed id: 7628012

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.