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5hek
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==crystal structure of M1.HpyAVI== | |
| + | <StructureSection load='5hek' size='340' side='right' caption='[[5hek]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == 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://oca.weizmann.ac.il/oca-docs/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> | ||
| + | <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=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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DNA 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<ref>PMID:27259995</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5hek" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Liu, W]] | [[Category: Liu, W]] | ||
| + | [[Category: Ma, B]] | ||
| + | [[Category: Zhang, H]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: M1 hpyavi]] | ||
Revision as of 03:25, 10 December 2016
crystal structure of M1.HpyAVI
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