5hek: Difference between revisions
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<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 with sequence from [ | <table><tr><td colspan='2'>[[5hek]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5HEK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hek OCA], [https://pdbe.org/5hek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hek RCSB], [https://www.ebi.ac.uk/pdbsum/5hek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hek ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O24891_HELPY O24891_HELPY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori 26695]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu | [[Category: Liu W]] | ||
[[Category: Ma | [[Category: Ma B]] | ||
[[Category: Zhang | [[Category: Zhang H]] | ||
Latest revision as of 10:33, 9 August 2023
crystal structure of M1.HpyAVIcrystal structure of M1.HpyAVI
Structural highlights
FunctionPublication 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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