1g60

<table><tr><td colspan='2'>[[1g60]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"haemophilus_bovis"_hauduroy_et_al._1937 "haemophilus bovis" hauduroy et al. 1937]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G60 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] </span></td></tr>

[[https://www.uniprot.org/uniprot/MTM2_MORBO MTM2_MORBO]] This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme.

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== Publication Abstract from PubMed ==

DNA methyltransferases (MTases) are sequence-specific enzymes which transfer a methyl group from S-adenosyl-L-methionine (AdoMet) to the amino group of either cytosine or adenine within a recognized DNA sequence. Methylation of a base in a specific DNA sequence protects DNA from nucleolytic cleavage by restriction enzymes recognizing the same DNA sequence. We have determined at 1.74 A resolution the crystal structure of a beta-class DNA MTase MboIIA (M.MboIIA) from the bacterium Moraxella bovis, the smallest DNA MTase determined to date. M.MboIIA methylates the 3' adenine of the pentanucleotide sequence 5'-GAAGA-3'. The protein crystallizes with two molecules in the asymmetric unit which we propose to resemble the dimer when M.MboIIA is not bound to DNA. The overall structure of the enzyme closely resembles that of M.RsrI. However, the cofactor-binding pocket in M.MboIIA forms a closed structure which is in contrast to the open-form structures of other known MTases.

Crystal structure of MboIIA methyltransferase.,Osipiuk J, Walsh MA, Joachimiak A Nucleic Acids Res. 2003 Sep 15;31(18):5440-8. PMID:12954781<ref>PMID:12954781</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Haemophilus bovis hauduroy et al. 1937]]

[[Category: Joachimiak, A]]

[[Category: Structural genomic]]

[[Category: Osipiuk, J]]

[[Category: Walsh, M A]]

[[Category: Transferase]]