1q0s

<StructureSection load='1q0s' size='340' side='right' caption='[[1q0s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[1q0s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0S FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0t|1q0t]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] </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=1q0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0s OCA], [http://pdbe.org/1q0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q0s RCSB], [http://www.ebi.ac.uk/pdbsum/1q0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q0s ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DMA_BPT4 DMA_BPT4]] This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.

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== Publication Abstract from PubMed ==

DNA-adenine methylation at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as bacterial virulence. We report here the crystal structures of the bacteriophage T4Dam DNA adenine methyltransferase (MTase) in a binary complex with the methyl-donor product S-adenosyl-L-homocysteine (AdoHcy) and in a ternary complex with a synthetic 12-bp DNA duplex and AdoHcy. T4Dam contains two domains: a seven-stranded catalytic domain that harbors the binding site for AdoHcy and a DNA binding domain consisting of a five-helix bundle and a beta-hairpin that is conserved in the family of GATC-related MTase orthologs. Unexpectedly, the sequence-specific T4Dam bound to DNA in a nonspecific mode that contained two Dam monomers per synthetic duplex, even though the DNA contains a single GATC site. The ternary structure provides a rare snapshot of an enzyme poised for linear diffusion along the DNA.

 

<div class="pdbe-citations 1q0s" style="background-color:#fffaf0;"></div>

== References ==

[[Category: Bpt4]]

[[Category: Cheng, X]]

[[Category: Dong, A]]

[[Category: Hattman, S]]

[[Category: Horton, J R]]

[[Category: Kossykh, V]]

[[Category: Schlagman, S L]]

[[Category: Yang, Z]]

[[Category: Zhang, X]]

[[Category: Zhang, X J]]

[[Category: Zhou, L]]

[[Category: Transferase]]