4rtj: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rtj RCSB], [http://www.ebi.ac.uk/pdbsum/4rtj PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rtj RCSB], [http://www.ebi.ac.uk/pdbsum/4rtj PDBsum]</span></td></tr>
</table>
</table>
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== Publication Abstract from PubMed ==
DNA adenine methyltransferase (Dam) is widespread and conserved among the gamma-proteobacteria. Methylation of the Ade in GATC sequences regulates diverse bacterial cell functions, including gene expression, mismatch repair and chromosome replication. Dam also controls virulence in many pathogenic Gram-negative bacteria. An unexplained and perplexing observation about Escherichia coli Dam (EcoDam) is that there is no obvious relationship between the genes that are transcriptionally responsive to Dam and the promoter-proximal presence of GATC sequences. Here, we demonstrate that EcoDam interacts with a 5-base pair non-cognate sequence distinct from GATC. The crystal structure of a non-cognate complex allowed us to identify a DNA binding element, GTYTA/TARAC (where Y = C/T and R = A/G). This element immediately flanks GATC sites in some Dam-regulated promoters, including the Pap operon which specifies pyelonephritis-associated pili. In addition, Dam interacts with near-cognate GATC sequences (i.e. 3/4-site ATC and GAT). Taken together, these results imply that Dam, in addition to being responsible for GATC methylation, could also function as a methylation-independent transcriptional repressor.
Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression.,Horton JR, Zhang X, Blumenthal RM, Cheng X Nucleic Acids Res. 2015 Apr 6. pii: gkv251. PMID:25845600<ref>PMID:25845600</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
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Revision as of 10:07, 22 April 2015

A non-cognate complex of Escherichia coli DNA Adenine Methyltransferase (DAM) with DNA and SinefunginA non-cognate complex of Escherichia coli DNA Adenine Methyltransferase (DAM) with DNA and Sinefungin

Structural highlights

4rtj is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

DNA adenine methyltransferase (Dam) is widespread and conserved among the gamma-proteobacteria. Methylation of the Ade in GATC sequences regulates diverse bacterial cell functions, including gene expression, mismatch repair and chromosome replication. Dam also controls virulence in many pathogenic Gram-negative bacteria. An unexplained and perplexing observation about Escherichia coli Dam (EcoDam) is that there is no obvious relationship between the genes that are transcriptionally responsive to Dam and the promoter-proximal presence of GATC sequences. Here, we demonstrate that EcoDam interacts with a 5-base pair non-cognate sequence distinct from GATC. The crystal structure of a non-cognate complex allowed us to identify a DNA binding element, GTYTA/TARAC (where Y = C/T and R = A/G). This element immediately flanks GATC sites in some Dam-regulated promoters, including the Pap operon which specifies pyelonephritis-associated pili. In addition, Dam interacts with near-cognate GATC sequences (i.e. 3/4-site ATC and GAT). Taken together, these results imply that Dam, in addition to being responsible for GATC methylation, could also function as a methylation-independent transcriptional repressor.

Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression.,Horton JR, Zhang X, Blumenthal RM, Cheng X Nucleic Acids Res. 2015 Apr 6. pii: gkv251. PMID:25845600[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Horton JR, Zhang X, Blumenthal RM, Cheng X. Structures of Escherichia coli DNA adenine methyltransferase (Dam) in complex with a non-GATC sequence: potential implications for methylation-independent transcriptional repression. Nucleic Acids Res. 2015 Apr 6. pii: gkv251. PMID:25845600 doi:http://dx.doi.org/10.1093/nar/gkv251

4rtj, resolution 1.99Å

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