1mht: Difference between revisions

Revision as of 23:59, 2 July 2008

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File:1mht.png

Template:STRUCTURE 1mht

COVALENT TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE, DNA AND S-ADENOSYL-L-HOMOCYSTEINECOVALENT TERNARY STRUCTURE OF HHAI METHYLTRANSFERASE, DNA AND S-ADENOSYL-L-HOMOCYSTEINE

Template:ABSTRACT PUBMED 8293469

About this StructureAbout this Structure

1MHT is a Single protein structure of sequence from Haemophilus haemolyticus. Full crystallographic information is available from OCA.

ReferenceReference

HhaI methyltransferase flips its target base out of the DNA helix., Klimasauskas S, Kumar S, Roberts RJ, Cheng X, Cell. 1994 Jan 28;76(2):357-69. PMID:8293469

Page seeded by OCA on Wed Jul 2 23:59:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
+<!--
-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.
+-->
+{{ABSTRACT_PUBMED_8293469}}
 ==About this Structure==
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 [[Category: Overhanging base]]
 [[Category: Protein-dna complex]]
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