2c7p: Difference between revisions
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==HhaI DNA methyltransferase complex with oligonucleotide containing 2- aminopurine opposite to the target base (GCGC:GMPC) and SAH== | ==HhaI DNA methyltransferase complex with oligonucleotide containing 2- aminopurine opposite to the target base (GCGC:GMPC) and SAH== | ||
<StructureSection load='2c7p' size='340' side='right' caption='[[2c7p]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2c7p' size='340' side='right' caption='[[2c7p]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[10mh|10mh]], [[1fjx|1fjx]], [[1hmy|1hmy]], [[1m0e|1m0e]], [[1mht|1mht]], [[1skm|1skm]], [[1svu|1svu]], [[2hmy|2hmy]], [[3mht|3mht]], [[4mht|4mht]], [[5mht|5mht]], [[6mht|6mht]], [[7mht|7mht]], [[8mht|8mht]], [[9mht|9mht]], [[2c7o|2c7o]], [[2c7q|2c7q]], [[2c7r|2c7r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[10mh|10mh]], [[1fjx|1fjx]], [[1hmy|1hmy]], [[1m0e|1m0e]], [[1mht|1mht]], [[1skm|1skm]], [[1svu|1svu]], [[2hmy|2hmy]], [[3mht|3mht]], [[4mht|4mht]], [[5mht|5mht]], [[6mht|6mht]], [[7mht|7mht]], [[8mht|8mht]], [[9mht|9mht]], [[2c7o|2c7o]], [[2c7q|2c7q]], [[2c7r|2c7r]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </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=2c7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7p OCA], [http://pdbe.org/2c7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7p RCSB], [http://www.ebi.ac.uk/pdbsum/2c7p 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=2c7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7p OCA], [http://pdbe.org/2c7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7p RCSB], [http://www.ebi.ac.uk/pdbsum/2c7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c7p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7p_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7p_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2c7p ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[DNA methyltransferase|DNA methyltransferase]] | *[[DNA methyltransferase|DNA methyltransferase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:48, 23 May 2018
HhaI DNA methyltransferase complex with oligonucleotide containing 2- aminopurine opposite to the target base (GCGC:GMPC) and SAHHhaI DNA methyltransferase complex with oligonucleotide containing 2- aminopurine opposite to the target base (GCGC:GMPC) and SAH
Structural highlights
Function[MTH1_HAEPH] This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDNA base flipping is an important mechanism in molecular enzymology, but its study is limited by the lack of an accessible and reliable diagnostic technique. A series of crystalline complexes of a DNA methyltransferase, M.HhaI, and its cognate DNA, in which a fluorescent nucleobase analogue, 2-aminopurine (AP), occupies defined positions with respect the target flipped base, have been prepared and their structures determined at higher than 2 A resolution. From time-resolved fluorescence measurements of these single crystals, we have established that the fluorescence decay function of AP shows a pronounced, characteristic response to base flipping: the loss of the very short (approximately 100 ps) decay component and the large increase in the amplitude of the long (approximately 10 ns) component. When AP is positioned at sites other than the target site, this response is not seen. Most significantly, we have shown that the same clear response is apparent when M.HhaI complexes with DNA in solution, giving an unambiguous signal of base flipping. Analysis of the AP fluorescence decay function reveals conformational heterogeneity in the DNA-enzyme complexes that cannot be discerned from the present X-ray structures. Time-resolved fluorescence of 2-aminopurine as a probe of base flipping in M.HhaI-DNA complexes.,Neely RK, Daujotyte D, Grazulis S, Magennis SW, Dryden DT, Klimasauskas S, Jones AC Nucleic Acids Res. 2005 Dec 9;33(22):6953-60. Print 2005. PMID:16340006[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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