3BVP

Crystal Structure of the N-terminal Catalytic Domain of TP901-1 Integrase

Summary for 3BVP

• Entry DOI: 10.2210/pdb3bvp/pdb
• Descriptor: TP901-1 Integrase (2 entities in total)
• Functional Keywords: dna recombinase, recombination
• Biological source: Lactococcus phage TP901-1
• Total number of polymer chains: 2
• Total formula weight: 31517.54

Authors

Yuan, P.,Van Duyne, G.D. (deposition date: 2008-01-07, release date: 2008-08-12, Last modification date: 2024-02-21)

Primary citation

Yuan, P.,Gupta, K.,Van Duyne, G.D.
Tetrameric structure of a serine integrase catalytic domain.
Structure, 16:1275-1286, 2008

PubMed Abstract: The serine integrases have recently emerged as powerful new chromosome engineering tools in various organisms and show promise for therapeutic use in human cells. The serine integrases are structurally and mechanistically unrelated to the bacteriophage lambda integrase but share a similar catalytic domain with the resolvase/invertase enzymes typified by the resolvase proteins from transposons Tn3 and gammadelta. Here we report the crystal structure and solution properties of the catalytic domain from bacteriophage TP901-1 integrase. The protein is a dimer in solution but crystallizes as a tetramer that is closely related in overall architecture to structures of activated gammadelta-resolvase mutants. The ability of the integrase tetramer to explain biochemical experiments performed in the resolvase and invertase systems suggests that the TP901 integrase tetramer represents a unique intermediate on the recombination pathway that is shared within the serine recombinase superfamily.

PubMed: 18682229
DOI: 10.1016/j.str.2008.04.018

Experimental method

X-RAY DIFFRACTION (2.1 Å)