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| [[Image:1nw7.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1nw7| PDB=1nw7 | SCENE= }} | | {{STRUCTURE_1nw7| PDB=1nw7 | SCENE= }} |
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| '''Structure of the beta class N6-adenine DNA methyltransferase RsrI bound to S-ADENOSYL-L-HOMOCYSTEINE'''
| | ===Structure of the beta class N6-adenine DNA methyltransferase RsrI bound to S-ADENOSYL-L-HOMOCYSTEINE=== |
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| ==Overview==
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| The structures of RsrI DNA methyltransferase (M.RsrI) bound to the substrate S-adenosyl-l-methionine (AdoMet), the product S-adenosyl-l-homocysteine (AdoHcy), the inhibitor sinefungin, as well as a mutant apo-enzyme have been determined by x-ray crystallography. Two distinct binding configurations were observed for the three ligands. The substrate AdoMet adopts a bent shape that directs the activated methyl group toward the active site near the catalytic DPPY motif. The product AdoHcy and the competitive inhibitor sinefungin bind with a straight conformation in which the amino acid moiety occupies a position near the activated methyl group in the AdoMet complex. Analysis of ligand binding in comparison with other DNA methyltransferases reveals a small, common subset of available conformations for the ligand. The structures of M.RsrI with the non-substrate ligands contained a bound chloride ion in the AdoMet carboxylate-binding pocket, explaining its inhibition by chloride salts. The L72P mutant of M.RsrI is the first DNA methyltransferase structure without bound ligand. With respect to the wild-type protein, it had a larger ligand-binding pocket and displayed movement of a loop (223-227) that is responsible for binding the ligand, which may account for the weaker affinity of the L72P mutant for AdoMet. These studies show the subtle changes in the tight specific interactions of substrate, product, and an inhibitor with M.RsrI and help explain how each displays its unique effect on the activity of the enzyme. | | The line below this paragraph, {{ABSTRACT_PUBMED_12732637}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12732637 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12732637}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rossmann fold]] | | [[Category: Rossmann fold]] |
| [[Category: S-adenosyl homocysteine]] | | [[Category: S-adenosyl homocysteine]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:03:07 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:31:05 2008'' |