2cdm: Difference between revisions

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[[Image:2cdm.gif|left|200px]]
{{Seed}}
[[Image:2cdm.png|left|200px]]


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{{STRUCTURE_2cdm|  PDB=2cdm  |  SCENE=  }}  
{{STRUCTURE_2cdm|  PDB=2cdm  |  SCENE=  }}  


'''THE STRUCTURE OF TRWC COMPLEXED WITH A 27-MER DNA COMPRISING THE RECOGNITION HAIRPIN AND THE CLEAVAGE SITE'''
===THE STRUCTURE OF TRWC COMPLEXED WITH A 27-MER DNA COMPRISING THE RECOGNITION HAIRPIN AND THE CLEAVAGE SITE===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16540117}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16540117 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16540117}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16540117 16540117]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16540117 16540117]
Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC., Guasch A, Lucas M, Moncalian G, Cabezas M, Perez-Luque R, Gomis-Ruth FX, de la Cruz F, Coll M, Nat Struct Biol. 2003 Dec;10(12):1002-10. Epub 2003 Nov 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14625590 14625590]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Dna-protein complex]]
[[Category: Dna-protein complex]]
[[Category: Relaxase]]
[[Category: Relaxase]]
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Revision as of 03:37, 29 July 2008

File:2cdm.png

Template:STRUCTURE 2cdm

THE STRUCTURE OF TRWC COMPLEXED WITH A 27-MER DNA COMPRISING THE RECOGNITION HAIRPIN AND THE CLEAVAGE SITE

Template:ABSTRACT PUBMED 16540117

About this Structure

2CDM is a Protein complex structure of sequences from Escherichia coli. 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

Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC., Guasch A, Lucas M, Moncalian G, Cabezas M, Perez-Luque R, Gomis-Ruth FX, de la Cruz F, Coll M, Nat Struct Biol. 2003 Dec;10(12):1002-10. Epub 2003 Nov 16. PMID:14625590

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