2cdm
From Proteopedia
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THE STRUCTURE OF TRWC COMPLEXED WITH A 27-MER DNA COMPRISING THE RECOGNITION HAIRPIN AND THE CLEAVAGE SITE
Overview
TrwC is a DNA strand transferase that catalyzes the initial and final, stages of conjugative DNA transfer. We have solved the crystal structure, of the N-terminal relaxase domain of TrwC in complex with a 27 base-long, DNA oligonucleotide that contains both the recognition hairpin and the, scissile phosphate. In addition, a series of ternary structures of, protein-DNA complexes with different divalent cations at the active site, have been solved. Systematic anomalous difference analysis allowed us to, determine unambiguously the nature of the metal bound. Zn2+, Ni2+ and Cu2+, were found to bind the histidine-triad metal binding site. Comparison of, the structures of the different complexes suggests two pathways for the, DNA to exit the active pocket. They are probably used at different ... [(full description)]
About this Structure
2CDM is a [Protein complex] structure of sequences from [Escherichia coli] with SO4 as [ligand]. Full crystallographic information is available from [OCA].
Reference
Unveiling the molecular mechanism of a conjugative relaxase: The structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site., Boer R, Russi S, Guasch A, Lucas M, Blanco AG, Perez-Luque R, Coll M, de la Cruz F, J Mol Biol. 2006 May 5;358(3):857-69. Epub 2006 Feb 28. PMID:16540117
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