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[[Image:1tw2.gif|left|200px]]
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[[Image:1tw2.png|left|200px]]


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{{STRUCTURE_1tw2|  PDB=1tw2  |  SCENE=  }}  
{{STRUCTURE_1tw2|  PDB=1tw2  |  SCENE=  }}  


'''Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET)'''
===Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET)===




==Overview==
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One of the final steps in the biosynthesis of the widely used anti-tumor drug daunorubicin in Streptomyces peucetius is the methylation of the 4-hydroxyl group of the tetracyclic ring system. This reaction is catalyzed by the S-adenosyl-L-methionine-dependent carminomycin 4-O-methyltransferase DnrK. The crystal structure of the ternary complex of this enzyme with the bound products S-adenosyl-L-homocysteine and 4-methoxy-epsilon-rhodomycin T has been determined to a 2.35-angstroms resolution. DnrK is a homodimer, and the subunit displays the typical fold of small molecule O-methyltransferases. The structure provides insights into the recognition of the anthracycline substrate and also suggests conformational changes as part of the catalytic cycle of the enzyme. The position and orientation of the bound ligands are consistent with an SN2 mechanism of methyl transfer. Mutagenesis experiments on a putative catalytic base confirm that DnrK most likely acts as an entropic enzyme in that rate enhancement is mainly due to orientational and proximity effects. This contrasts the mechanism of DnrK with that of other O-methyltransferases where acid/base catalysis has been demonstrated to be an essential contribution to rate enhancement.
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{{ABSTRACT_PUBMED_15273252}}


==About this Structure==
==About this Structure==
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[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
[[Category: Tailoring enzyme]]
[[Category: Tailoring enzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:12:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:37:53 2008''

Revision as of 11:37, 27 July 2008

File:1tw2.png

Template:STRUCTURE 1tw2

Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET)

Template:ABSTRACT PUBMED 15273252

About this Structure

1TW2 is a Single protein structure of sequence from Streptomyces peucetius. Full crystallographic information is available from OCA.

Reference

Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products., Jansson A, Koskiniemi H, Mantsala P, Niemi J, Schneider G, J Biol Chem. 2004 Sep 24;279(39):41149-56. Epub 2004 Jul 24. PMID:15273252

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