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New page: left|200px<br /><applet load="2dpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dpm, resolution 1.8Å" /> '''DPNM DNA ADENINE METH...
 
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[[Image:2dpm.gif|left|200px]]<br /><applet load="2dpm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2dpm, resolution 1.8&Aring;" />
'''DPNM DNA ADENINE METHYLTRANSFERASE FROM STREPTOCCOCUS PNEUMONIAE COMPLEXED WITH S-ADENOSYLMETHIONINE'''<br />


==Overview==
==DPNM DNA ADENINE METHYLTRANSFERASE FROM STREPTOCCOCUS PNEUMONIAE COMPLEXED WITH S-ADENOSYLMETHIONINE==
Background:. Methyltransferases (Mtases) catalyze the transfer of methyl, groups from S-adenosylmethionine (AdoMet) to a variety of small molecular, and macromolecular substrates. These enzymes contain a characteristic, alpha/beta structural fold. Four groups of DNA Mtases have been defined, and representative structures have been determined for three groups. DpnM, is a DNA Mtase that acts on adenine N6 in the sequence GATC; the enzyme, represents group alpha DNA Mtases, for which no structures are known., Results:. The structure of DpnM in complex with AdoMet was determined at, 1.80 A resolution. The protein comprises a consensus Mtase fold with a, helical cluster insert. DpnM binds AdoMet in a similar manner to most, other Mtases and the enzyme contains a hollow that can accommodate DNA., The helical cluster supports a shelf within the hollow that may recognize, the target sequence. Modeling studies indicate a potential site for, binding the target adenine, everted from the DNA helix. Comparison of the, DpnM structure and sequences of group alpha DNA Mtases indicates that the, group is a genetically related family. Structural comparisons show DpnM to, be most similar to a small-molecule Mtase and then to macromolecular, Mtases, although several dehydrogenases show greater similarity than one, DNA Mtase. Conclusions:. DpnM, and by extension the DpnM family or group, alpha Mtases, contains the consensus fold and AdoMet-binding motifs found, in most Mtases. Structural considerations suggest that macromolecular, Mtases evolved from small-molecule Mtases, with different groups of DNA, Mtases evolving independently. Mtases may have evolved from, dehydrogenases. Comparison of these enzymes indicates that in protein, evolution, the structural fold is most highly conserved, then function and, lastly sequence.
<StructureSection load='2dpm' size='340' side='right'caption='[[2dpm]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2dpm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DPM FirstGlance]. <br>
2DPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with HG and SAM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DPM OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpm OCA], [https://pdbe.org/2dpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpm RCSB], [https://www.ebi.ac.uk/pdbsum/2dpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpm ProSAT]</span></td></tr>
Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine., Tran PH, Korszun ZR, Cerritelli S, Springhorn SS, Lacks SA, Structure. 1998 Dec 15;6(12):1563-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9862809 9862809]
</table>
[[Category: Single protein]]
== Function ==
[[Category: Site-specific DNA-methyltransferase (adenine-specific)]]
[https://www.uniprot.org/uniprot/MTD21_STREE MTD21_STREE] This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the DpnII endonuclease.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/2dpm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dpm ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
[[Category: Cerritelli, S.]]
[[Category: Cerritelli S]]
[[Category: Korszun, Z.R.]]
[[Category: Korszun ZR]]
[[Category: Lacks, S.A.]]
[[Category: Lacks SA]]
[[Category: Springhorn, S.S.]]
[[Category: Springhorn SS]]
[[Category: Tran, P.H.]]
[[Category: Tran PH]]
[[Category: HG]]
[[Category: SAM]]
[[Category: dna adenine methyltransferase]]
[[Category: dna methyltransferase group alpha]]
[[Category: dna n6-adenine methylation]]
[[Category: dpnii restriction-modification system]]
[[Category: gatc methylation]]
[[Category: methylase]]
[[Category: methyltransferase]]
[[Category: rossman fold]]
[[Category: s-adenosylmethionine]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:42:36 2007''

Latest revision as of 09:18, 14 February 2024

DPNM DNA ADENINE METHYLTRANSFERASE FROM STREPTOCCOCUS PNEUMONIAE COMPLEXED WITH S-ADENOSYLMETHIONINE

2dpm, resolution 1.80Å

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