Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration.

Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration.

Abstr Meet Groups Stud Struct AIDS Relat Syst Their Appl Target Drug Des. 1995 Jun 5-7;9:(unnumbered abstract). Unique Identifier : AIDSLINE AIDS/96095610
Rice P

Abstract: The crystal structure of the core domain of bacteriophage Mu transposase, MuA, has been determined at 2.4A 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, RNAseH and RuvC. The second subdomain is a 6-stranded antiparallel beta barrel, and connects to the first 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 crosstalk between the active site and the other domains of the transposase that controls the activity of the protein.

Keywords: Bacterial Proteins/CHEMISTRY Bacteriophage mu/*ENZYMOLOGY/PHYSIOLOGY Binding Sites Comparative Study Crystallography, X-Ray DNA Nucleotidyltransferases/*CHEMISTRY/PHYSIOLOGY DNA, Viral/*METABOLISM Endodeoxyribonucleases/CHEMISTRY HIV-1/ENZYMOLOGY Molecular Structure Protein Conformation Ribonuclease H, Calf Thymus/CHEMISTRY Virus Integration/*PHYSIOLOGY ABSTRACT
960730
M9670105

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