1aqi
From Proteopedia
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'''STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI''' | '''STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI''' | ||
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Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI., Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W, J Mol Biol. 1997 Jan 10;265(1):56-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8995524 8995524] | Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI., Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W, J Mol Biol. 1997 Jan 10;265(1):56-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8995524 8995524] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Site-specific DNA-methyltransferase (adenine-specific)]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
[[Category: Schluckebier, G.]] | [[Category: Schluckebier, G.]] | ||
| - | [[Category: | + | [[Category: Methyltransferase]] |
| - | [[Category: | + | [[Category: Restriction system]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:35:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:35, 2 May 2008
STRUCTURE OF ADENINE-N6-DNA-METHYLTRANSFERASE TAQI
Overview
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.
About this Structure
1AQI is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI., Schluckebier G, Kozak M, Bleimling N, Weinhold E, Saenger W, J Mol Biol. 1997 Jan 10;265(1):56-67. PMID:8995524 Page seeded by OCA on Fri May 2 10:35:13 2008
