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| [[Image:1mht.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mht| PDB=1mht | SCENE= }} | | {{STRUCTURE_1mht| PDB=1mht | SCENE= }} |
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| '''COVALENT TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE, DNA AND S-ADENOSYL-L-HOMOCYSTEINE'''
| | ===COVALENT TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE, DNA AND S-ADENOSYL-L-HOMOCYSTEINE=== |
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| ==Overview==
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| The crystal structure has been determined at 2.8 A resolution for a chemically-trapped covalent reaction intermediate between the HhaI DNA cytosine-5-methyltransferase, S-adenosyl-L-homocysteine, and a duplex 13-mer DNA oligonucleotide containing methylated 5-fluorocytosine at its target. The DNA is located in a cleft between the two domains of the protein and has the characteristic conformation of B-form DNA, except for a disrupted G-C base pair that contains the target cytosine. The cytosine residue has swung completely out of the DNA helix and is positioned in the active site, which itself has undergone a large conformational change. The DNA is contacted from both the major and the minor grooves, but almost all base-specific interactions between the enzyme and the recognition bases occur in the major groove, through two glycine-rich loops from the small domain. The structure suggests how the active nucleophile reaches its target, directly supports the proposed mechanism for cytosine-5 DNA methylation, and illustrates a novel mode of sequence-specific DNA recognition. | | The line below this paragraph, {{ABSTRACT_PUBMED_8293469}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8293469 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8293469}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Overhanging base]] | | [[Category: Overhanging base]] |
| [[Category: Protein-dna complex]] | | [[Category: Protein-dna complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:03:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:59:42 2008'' |
