2cdm
From Proteopedia
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==Overview== | ==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 . | + | 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 steps, of the conjugative DNA-processing reaction. The structural information, allows us to propose (i) an enzyme mechanism where the scissile phosphate, is polarized by the metal ion facilitating the nucleophilic attack of the, catalytic tyrosine, and (ii) a probable sequence of events during, conjugative DNA processing that explains the biological function of the, relaxase. |
==About this Structure== | ==About this Structure== | ||
| - | 2CDM is a | + | 2CDM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CDM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: relaxase]] | [[Category: relaxase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:37:29 2007'' |
Revision as of 11:32, 5 November 2007
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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 steps, of the conjugative DNA-processing reaction. The structural information, allows us to propose (i) an enzyme mechanism where the scissile phosphate, is polarized by the metal ion facilitating the nucleophilic attack of the, catalytic tyrosine, and (ii) a probable sequence of events during, conjugative DNA processing that explains the biological function of the, relaxase.
About this Structure
2CDM is a Protein complex structure of sequences from Escherichia coli with SO4 as ligand. Structure known Active Site: AC1. 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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