1QX0

CONJUGATIVE RELAXASE TRWC IN COMPLEX WITH ORIT DNA. METAL-BOUND STRUCTURE

Summary for 1QX0

• Entry DOI: 10.2210/pdb1qx0/pdb
• Related: 1omh 1osb
• Descriptor: DNA OLIGONUCLEOTIDE, trwC protein, SULFATE ION, ... (5 entities in total)
• Functional Keywords: protein-dna complex, bacterial conjugation, relaxase, dna replication, transferase-dna complex, transferase/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 40958.86

Authors

Guasch, A.,Lucas, M.,Moncalian, G.,Cabezas, M.,Prez-Luque, R.,Gomis-Rth, F.X.,de la Cruz, F.,Coll, M. (deposition date: 2003-09-04, release date: 2003-11-25, Last modification date: 2024-10-30)

Primary citation

Guasch, A.,Lucas, M.,Moncalian, G.,Cabezas, M.,Prez-Luque, R.,Gomis-Rth, F.X.,de la Cruz, F.,Coll, M.
RECOGNITION AND PROCESSING OF THE ORIGIN OF TRANSFER DNA BY CONJUGATIVE RELAXASE TRWC
Nat.Struct.Biol., 10:1002-1010, 2003

PubMed Abstract: Relaxases are DNA strand transferases that catalyze the initial and final stages of DNA processing during conjugative cell-to-cell DNA transfer. Upon binding to the origin of transfer (oriT) DNA, relaxase TrwC melts the double helix. The three-dimensional structure of the relaxase domain of TrwC in complex with its cognate DNA at oriT shows a fold built on a two-layer alpha/beta sandwich, with a deep narrow cleft that houses the active site. The DNA includes one arm of an extruded cruciform, an essential feature for specific recognition. This arm is firmly embraced by the protein through a beta-ribbon positioned in the DNA major groove and a loop occupying the minor groove. It is followed by a single-stranded DNA segment that enters the active site, after a sharp U-turn forming a hydrophobic cage that traps the N-terminal methionine. Structural analysis combined with site-directed mutagenesis defines the architecture of the active site.

PubMed: 14625590
DOI: 10.1038/nsb1017

Experimental method

X-RAY DIFFRACTION (2.26 Å)