2zcj

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[[Image:2zcj.gif|left|200px]]
[[Image:2zcj.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2zcj |SIZE=350|CAPTION= <scene name='initialview01'>2zcj</scene>, resolution 2.75&Aring;
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The line below this paragraph, containing "STRUCTURE_2zcj", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= hhaIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=735 Haemophilus parahaemolyticus])
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-->
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|DOMAIN=
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{{STRUCTURE_2zcj| PDB=2zcj | SCENE= }}
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|RELATEDENTRY=[[2hr1|2HR1]], [[2z6u|2Z6U]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zcj OCA], [http://www.ebi.ac.uk/pdbsum/2zcj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zcj RCSB]</span>
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}}
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'''Ternary structure of the Glu119Gln M.HhaI, C5-Cytosine DNA methyltransferase, with unmodified DNA and AdoHcy'''
'''Ternary structure of the Glu119Gln M.HhaI, C5-Cytosine DNA methyltransferase, with unmodified DNA and AdoHcy'''
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==Reference==
==Reference==
AdoMet-dependent methyl-transfer: Glu119 is essential for DNA C5-cytosine methyltransferase M.HhaI., Shieh FK, Reich NO, J Mol Biol. 2007 Nov 9;373(5):1157-68. Epub 2007 Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17897676 17897676]
AdoMet-dependent methyl-transfer: Glu119 is essential for DNA C5-cytosine methyltransferase M.HhaI., Shieh FK, Reich NO, J Mol Biol. 2007 Nov 9;373(5):1157-68. Epub 2007 Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17897676 17897676]
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[[Category: DNA (cytosine-5-)-methyltransferase]]
 
[[Category: Haemophilus parahaemolyticus]]
[[Category: Haemophilus parahaemolyticus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Shieh, F K.]]
[[Category: Shieh, F K.]]
[[Category: 3-layer sandwich]]
[[Category: 3-layer sandwich]]
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[[Category: alpha and beta]]
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[[Category: Alpha and beta]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: restriction system]]
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[[Category: Restriction system]]
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[[Category: s-adenosyl-l-methionine]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: transferase/dna complex]]
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[[Category: Transferase/dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:08:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:20:20 2008''
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Revision as of 17:08, 4 May 2008

Template:STRUCTURE 2zcj

Ternary structure of the Glu119Gln M.HhaI, C5-Cytosine DNA methyltransferase, with unmodified DNA and AdoHcy


Overview

The role of Glu119 in S-adenosyl-L-methionine-dependent DNA methyltransferase M.HhaI-catalyzed DNA methylation was studied. Glu119 belongs to the highly conserved Glu/Asn/Val motif found in all DNA C5-cytosine methyltransferases, and its importance for M.HhaI function remains untested. We show that formation of the covalent intermediate between Cys81 and the target cytosine requires Glu119, since conversion to Ala, Asp or Gln lowers the rate of methyl transfer 10(2)-10(6) fold. Further, unlike the wild-type M.HhaI, these mutants are not trapped by the substrate in which the target cytosine is replaced with the mechanism-based inhibitor 5-fluorocytosine. The DNA binding affinity for the Glu119Asp mutant is decreased 10(3)-fold. Thus, the ability of the enzyme to stabilize the extrahelical cytosine is coupled directly to tight DNA binding. The structures of the ternary protein/DNA/AdoHcy complexes for both the Glu119Ala and Glu119Gln mutants (2.70 A and 2.75 A, respectively) show that the flipped base is positioned nearly identically with that observed in the wild-type M.HhaI complex. A single water molecule in the Glu119Ala structure between Ala119 and the extrahelical cytosine N3 is lacking in the Glu119Gln and wild-type M.HhaI structures, and most likely accounts for this mutant's partial activity. Glu119 has essential roles in activating the target cytosine for nucleophilic attack and contributes to tight DNA binding.

About this Structure

2ZCJ is a Protein complex structure of sequences from Haemophilus parahaemolyticus. Full crystallographic information is available from OCA.

Reference

AdoMet-dependent methyl-transfer: Glu119 is essential for DNA C5-cytosine methyltransferase M.HhaI., Shieh FK, Reich NO, J Mol Biol. 2007 Nov 9;373(5):1157-68. Epub 2007 Aug 19. PMID:17897676 Page seeded by OCA on Sun May 4 20:08:54 2008

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