5hek: Difference between revisions
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==crystal structure of M1.HpyAVI== | ==crystal structure of M1.HpyAVI== | ||
<StructureSection load='5hek' size='340' side='right' caption='[[5hek]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='5hek' size='340' side='right'caption='[[5hek]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hek]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HEK OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5hek]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HEK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HEK FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hfj|5hfj]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hfj|5hfj]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hek OCA], [http://pdbe.org/5hek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hek RCSB], [http://www.ebi.ac.uk/pdbsum/5hek PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hek ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5hek" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5hek" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Campylobacter pylori]] | |||
[[Category: Large Structures]] | |||
[[Category: Liu, W]] | [[Category: Liu, W]] | ||
[[Category: Ma, B]] | [[Category: Ma, B]] | ||
Revision as of 10:02, 20 May 2020
crystal structure of M1.HpyAVIcrystal structure of M1.HpyAVI
Structural highlights
Publication Abstract from PubMedDNA N6-methyladenine modification plays an important role in regulating a variety of biological functions in bacteria. However, the mechanism of sequence-specific recognition in N6-methyladenine modification remains elusive. M1.HpyAVI, a DNA N6-adenine methyltransferase from Helicobacter pylori, shows more promiscuous substrate specificity than other enzymes. Here, we present the crystal structures of cofactor-free and AdoMet-bound structures of this enzyme, which were determined at resolutions of 3.0 A and 3.1 A, respectively. The core structure of M1.HpyAVI resembles the canonical AdoMet-dependent MTase fold, while the putative DNA binding regions considerably differ from those of the other MTases, which may account for the substrate promiscuity of this enzyme. Site-directed mutagenesis experiments identified residues D29 and E216 as crucial amino acids for cofactor binding and the methyl transfer activity of the enzyme, while P41, located in a highly flexible loop, playing a determinant role for substrate specificity. Taken together, our data revealed the structural basis underlying DNA N6-adenine methyltransferase substrate promiscuity. Biochemical and structural characterization of a DNA N6-adenine methyltransferase from Helicobacter pylori.,Ma B, Ma J, Liu D, Guo L, Chen H, Ding J, Liu W, Zhang H Oncotarget. 2016 Jul 5;7(27):40965-40977. doi: 10.18632/oncotarget.9692. PMID:27259995[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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