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| {{STRUCTURE_2adm| PDB=2adm | SCENE= }} | | {{STRUCTURE_2adm| PDB=2adm | SCENE= }} |
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| '''ADENINE-N6-DNA-METHYLTRANSFERASE TAQI'''
| | ===ADENINE-N6-DNA-METHYLTRANSFERASE TAQI=== |
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| ==Overview==
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| The crystal structures of the binary complexes of the DNA methyltransferase M.TaqI with the inhibitor Sinefungin and the reaction product S-adenosyl-L-homocysteine were determined, both at 2.6 A resolution. Structural comparison of these binary complexes with the complex formed by M.TaqI and the cofactor S-adenosyl-L-methionine suggests that the key element for molecular recognition of these ligands is the binding of their adenosine part in a pocket, and discrimination between cofactor, reaction product and inhibitor is mediated by different conformations of these molecules; the methionine part of S-adenosyl-L-methionine is located in the binding cleft, whereas the amino acid moieties of Sinefungin and S-adenosyl-L-homocysteine are in a different orientation and interact with the active site amino acid residues 105NPPY108. Dissociation constants for the complexes of M.TaqI with the three ligands were determined spectrofluorometrically. Sinefungin binds more strongly than S-adenosyl-L-homocysteine or S-adenosyl-L-methionine, with KD=0.34 microM, 2.4 microM and 2.0 microM, respectively. | | The line below this paragraph, {{ABSTRACT_PUBMED_8995524}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8995524 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8995524}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Restriction system]] | | [[Category: Restriction system]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:54:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:59:02 2008'' |