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| <StructureSection load='6k0w' size='340' side='right'caption='[[6k0w]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='6k0w' size='340' side='right'caption='[[6k0w]], [[Resolution|resolution]] 2.65Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6k0w]] 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=6K0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k0w]] 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=6K0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K0W FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0593 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene></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=6k0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k0w OCA], [http://pdbe.org/6k0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k0w RCSB], [http://www.ebi.ac.uk/pdbsum/6k0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k0w ProSAT]</span></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=6k0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k0w OCA], [https://pdbe.org/6k0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k0w RCSB], [https://www.ebi.ac.uk/pdbsum/6k0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k0w ProSAT]</span></td></tr> |
| </table> | | </table> |
- | <div style="background-color:#fffaf0;">
| + | == Function == |
- | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/O25315_HELPY O25315_HELPY] |
- | Methylation of genomic DNA can influence the transcription profile of an organism and may generate phenotypic diversity for rapid adaptation in a dynamic environment. M.HpyAXI is a Type III DNA methyltransferase present in Helicobacter pylori and is upregulated at low pH. This enzyme may alter the expression of critical genes to ensure the survival of this pathogen at low pH inside the human stomach. M.HpyAXI methylates the adenine in the target sequence (5'-GCAG-3') and shows maximal activity at pH 5.5. Type III DNA methyltransferases are found to form an inverted dimer in the functional form. We observe that M.HpyAXI forms a nonfunctional dimer at pH 8.0 that is incapable of DNA binding and methylation activity. However, at pH 5.5, two such dimers associate to form a tetramer that now includes two functional dimers that can bind and methylate the target DNA sequence. Overall, we observe that the pH-dependent tetramerization of M.HpyAXI ensures that the enzyme is licensed to act only in the presence of acid stress.
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- | | + | |
- | Tetramerization at Low pH Licenses DNA Methylation Activity of M.HpyAXI in the Presence of Acid Stress.,Narayanan N, Banerjee A, Jain D, Kulkarni DS, Sharma R, Nirwal S, Rao DN, Nair DT J Mol Biol. 2019 Oct 16. pii: S0022-2836(19)30579-0. doi:, 10.1016/j.jmb.2019.10.001. PMID:31628946<ref>PMID:31628946</ref>
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- | | + | |
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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- | </div>
| + | |
- | <div class="pdbe-citations 6k0w" style="background-color:#fffaf0;"></div>
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- | == References ==
| + | |
- | <references/>
| + | |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Nair, D T]] | + | [[Category: Nair DT]] |
- | [[Category: Narayanan, N]] | + | [[Category: Narayanan N]] |
- | [[Category: Dna binding protein]]
| + | |
- | [[Category: Dna methyltransferase]]
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- | [[Category: Sinefungin]]
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