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| | <StructureSection load='1boo' size='340' side='right'caption='[[1boo]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1boo' size='340' side='right'caption='[[1boo]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1boo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1boo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOO 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]] 2.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(cytosine-N(4)-specific) Site-specific DNA-methyltransferase (cytosine-N(4)-specific)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.113 2.1.1.113] </span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1boo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boo OCA], [https://pdbe.org/1boo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1boo RCSB], [https://www.ebi.ac.uk/pdbsum/1boo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1boo 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=1boo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1boo OCA], [https://pdbe.org/1boo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1boo RCSB], [https://www.ebi.ac.uk/pdbsum/1boo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1boo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MTP2_PROHU MTP2_PROHU]] This methylase recognizes the double-stranded sequence CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.
| + | [https://www.uniprot.org/uniprot/MTP2_PROHU MTP2_PROHU] This methylase recognizes the double-stranded sequence CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Blumenthal, R M]] | + | [[Category: Proteus vulgaris]] |
| - | [[Category: Cheng, X]] | + | [[Category: Blumenthal RM]] |
| - | [[Category: Gara, M O]] | + | [[Category: Cheng X]] |
| - | [[Category: Gong, W]] | + | [[Category: Gong W]] |
| - | [[Category: Amino methylation]] | + | [[Category: O'Gara M]] |
| - | [[Category: Multiwavelength anomalous diffraction]]
| + | |
| - | [[Category: Selenomethionine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MTP2_PROHU This methylase recognizes the double-stranded sequence CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We have determined the structure of Pvu II methyltransferase (M. Pvu II) complexed with S -adenosyl-L-methionine (AdoMet) by multiwavelength anomalous diffraction, using a crystal of the selenomethionine-substituted protein. M. Pvu II catalyzes transfer of the methyl group from AdoMet to the exocyclic amino (N4) nitrogen of the central cytosine in its recognition sequence 5'-CAGCTG-3'. The protein is dominated by an open alpha/beta-sheet structure with a prominent V-shaped cleft: AdoMet and catalytic amino acids are located at the bottom of this cleft. The size and the basic nature of the cleft are consistent with duplex DNA binding. The target (methylatable) cytosine, if flipped out of the double helical DNA as seen for DNA methyltransferases that generate 5-methylcytosine, would fit into the concave active site next to the AdoMet. This M. Pvu IIalpha/beta-sheet structure is very similar to those of M. Hha I (a cytosine C5 methyltransferase) and M. Taq I (an adenine N6 methyltransferase), consistent with a model predicting that DNA methyltransferases share a common structural fold while having the major functional regions permuted into three distinct linear orders. The main feature of the common fold is a seven-stranded beta-sheet (6 7 5 4 1 2 3) formed by five parallel beta-strands and an antiparallel beta-hairpin. The beta-sheet is flanked by six parallel alpha-helices, three on each side. The AdoMet binding site is located at the C-terminal ends of strands beta1 and beta2 and the active site is at the C-terminal ends of strands beta4 and beta5 and the N-terminal end of strand beta7. The AdoMet-protein interactions are almost identical among M. Pvu II, M. Hha I and M. Taq I, as well as in an RNA methyltransferase and at least one small molecule methyltransferase. The structural similarity among the active sites of M. Pvu II, M. Taq I and M. Hha I reveals that catalytic amino acids essential for cytosine N4 and adenine N6 methylation coincide spatially with those for cytosine C5 methylation, suggesting a mechanism for amino methylation.
Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment.,Gong W, O'Gara M, Blumenthal RM, Cheng X Nucleic Acids Res. 1997 Jul 15;25(14):2702-15. PMID:9207015[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gong W, O'Gara M, Blumenthal RM, Cheng X. Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. Nucleic Acids Res. 1997 Jul 15;25(14):2702-15. PMID:9207015
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