5hfj: Difference between revisions

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'''Unreleased structure'''


The entry 5hfj is ON HOLD  until Paper Publication
==crystal structure of M1.HpyAVI-SAM complex==
<StructureSection load='5hfj' size='340' side='right' caption='[[5hfj]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hfj]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HFJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hek|5hek]]</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=5hfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hfj OCA], [http://pdbe.org/5hfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hfj RCSB], [http://www.ebi.ac.uk/pdbsum/5hfj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hfj 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.


Authors: Ma, B., Liu, W., Zhang, H.
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>


Description: crystal structure of M1.HpyAVI-SAM complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5hfj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Liu, W]]
[[Category: Ma, B]]
[[Category: Zhang, H]]
[[Category: Zhang, H]]
[[Category: Ma, B]]
[[Category: Dna binding protein]]
[[Category: Liu, W]]
[[Category: M1 hpyavi]]
[[Category: Sam]]
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