1dct
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dct]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_biotype_aegyptius Haemophilus influenzae biotype aegyptius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCT FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dct]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_biotype_aegyptius Haemophilus influenzae biotype aegyptius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCT FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </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=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=C49:4-THIO,5-FLUORO,5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>C49</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dct OCA], [https://pdbe.org/1dct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dct RCSB], [https://www.ebi.ac.uk/pdbsum/1dct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dct 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=1dct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dct OCA], [https://pdbe.org/1dct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dct RCSB], [https://www.ebi.ac.uk/pdbsum/1dct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dct ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/MTH3_HAEAE MTH3_HAEAE] This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the HaeIII endonuclease. | |
== 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=1dct 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=1dct ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Many organisms expand the information content of their genome through enzymatic methylation of cytosine residues. Here we report the 2.8 A crystal structure of a bacterial DNA (cytosine-5)-methyltransferase (DCMtase), M. HaeIII, bound covalently to DNA. In this complex, the substrate cytosine is extruded from the DNA helix and inserted into the active site of the enzyme, as has been observed for another DCMtase, M. HhaI. The DNA is bound in a cleft between the two domains of the protein and is distorted from the characteristic B-form conformation at its recognition sequence. A comparison of structures shows a variation in the mode of DNA recognition: M. HaeIII differs from M. HhaI in that the remaining bases in its recognition sequence undergo an extensive rearrangement in their pairing. In this process, the bases are unstacked, and a gap 8 A long opens in the DNA. | ||
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| - | The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing.,Reinisch KM, Chen L, Verdine GL, Lipscomb WN Cell. 1995 Jul 14;82(1):143-53. PMID:7606780<ref>PMID:7606780</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dct" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Haemophilus influenzae biotype aegyptius]] | [[Category: Haemophilus influenzae biotype aegyptius]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chen | + | [[Category: Chen L]] |
| - | [[Category: Lipscomb | + | [[Category: Lipscomb WN]] |
| - | [[Category: Reinisch | + | [[Category: Reinisch KM]] |
| - | [[Category: Verdine | + | [[Category: Verdine GL]] |
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Revision as of 09:49, 20 March 2024
DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA
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