6k0w

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'''Unreleased structure'''
 
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The entry 6k0w is ON HOLD until Paper Publication
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==DNA methyltransferase in complex with sinefungin==
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<StructureSection load='6k0w' size='340' side='right'caption='[[6k0w]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6k0w]] is a 4 chain structure. 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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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Authors: Narayanan, N., Nair, D.T.
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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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Description: DNA methyltransferase in complex with sinefungin
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Nair, D.T]]
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<div class="pdbe-citations 6k0w" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Nair, D T]]
[[Category: Narayanan, N]]
[[Category: Narayanan, N]]
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[[Category: Dna binding protein]]
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[[Category: Dna methyltransferase]]
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[[Category: Sinefungin]]

Revision as of 15:05, 11 December 2019

DNA methyltransferase in complex with sinefungin

PDB ID 6k0w

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