1q0s: Difference between revisions

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<StructureSection load='1q0s' size='340' side='right'caption='[[1q0s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1q0s' size='340' side='right'caption='[[1q0s]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1q0s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q0S FirstGlance]. <br>
<table><tr><td colspan='2'>[[1q0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q0S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q0t|1q0t]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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=1q0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0s OCA], [https://pdbe.org/1q0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q0s RCSB], [https://www.ebi.ac.uk/pdbsum/1q0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q0s ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0s OCA], [http://pdbe.org/1q0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q0s RCSB], [http://www.ebi.ac.uk/pdbsum/1q0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q0s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DMA_BPT4 DMA_BPT4]] This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.  
[https://www.uniprot.org/uniprot/DMA_BPT4 DMA_BPT4] This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q0s ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q0s ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA-adenine methylation at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as bacterial virulence. We report here the crystal structures of the bacteriophage T4Dam DNA adenine methyltransferase (MTase) in a binary complex with the methyl-donor product S-adenosyl-L-homocysteine (AdoHcy) and in a ternary complex with a synthetic 12-bp DNA duplex and AdoHcy. T4Dam contains two domains: a seven-stranded catalytic domain that harbors the binding site for AdoHcy and a DNA binding domain consisting of a five-helix bundle and a beta-hairpin that is conserved in the family of GATC-related MTase orthologs. Unexpectedly, the sequence-specific T4Dam bound to DNA in a nonspecific mode that contained two Dam monomers per synthetic duplex, even though the DNA contains a single GATC site. The ternary structure provides a rare snapshot of an enzyme poised for linear diffusion along the DNA.
Structure of the bacteriophage T4 DNA adenine methyltransferase.,Yang Z, Horton JR, Zhou L, Zhang XJ, Dong A, Zhang X, Schlagman SL, Kossykh V, Hattman S, Cheng X Nat Struct Biol. 2003 Oct;10(10):849-55. Epub 2003 Aug 24. PMID:12937411<ref>PMID:12937411</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1q0s" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[DNA adenine methylase|DNA adenine methylase]]
*[[DNA adenine methylase|DNA adenine methylase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cheng, X]]
[[Category: Cheng X]]
[[Category: Dong, A]]
[[Category: Dong A]]
[[Category: Hattman, S]]
[[Category: Hattman S]]
[[Category: Horton, J R]]
[[Category: Horton JR]]
[[Category: Kossykh, V]]
[[Category: Kossykh V]]
[[Category: Schlagman, S L]]
[[Category: Schlagman SL]]
[[Category: Yang, Z]]
[[Category: Yang Z]]
[[Category: Zhang, X]]
[[Category: Zhang X]]
[[Category: Zhang, X J]]
[[Category: Zhang XJ]]
[[Category: Zhou, L]]
[[Category: Zhou L]]
[[Category: Methyltransferase]]
[[Category: T4dam]]
[[Category: Transferase]]

Latest revision as of 11:12, 14 February 2024

Binary Structure of T4DAM with AdoHcyBinary Structure of T4DAM with AdoHcy

Structural highlights

1q0s is a 1 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DMA_BPT4 This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1q0s, resolution 2.30Å

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OCA