1qzz

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{{STRUCTURE_1qzz| PDB=1qzz | SCENE= }}
{{STRUCTURE_1qzz| PDB=1qzz | SCENE= }}
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'''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)'''
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===Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)===
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==Overview==
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Anthracyclines are aromatic polyketide antibiotics, and several of these compounds are widely used as anti-tumor drugs in chemotherapy. Aclacinomycin-10-hydroxylase (RdmB) is one of the tailoring enzymes that modify the polyketide backbone in the biosynthesis of these metabolites. RdmB, a S-adenosyl-L-methionine-dependent methyltransferase homolog, catalyses the hydroxylation of 15-demethoxy-epsilon-rhodomycin to beta-rhodomycin, one step in rhodomycin biosynthesis in Streptomyces purpurascens. The crystal structure of RdmB, determined by multiwavelength anomalous diffraction to 2.1A resolution, reveals that the enzyme subunit has a fold similar to methyltransferases and binds S-adenosyl-L-methionine. The N-terminal domain, which consists almost exclusively of alpha-helices, is involved in dimerization. The C-terminal domain contains a typical alpha/beta nucleotide-binding fold, which binds S-adenosyl-L-methionine, and several of the residues interacting with the cofactor are conserved in O-methyltransferases. Adjacent to the S-adenosyl-L-methionine molecule there is a large cleft extending to the enzyme surface of sufficient size to bind the substrate. Analysis of the putative substrate-binding pocket suggests that there is no enzymatic group in proximity of the substrate 15-demethoxy-epsilon-rhodomycin, which could assist in proton abstraction and thus facilitate methyl transfer. The lack of a suitably positioned catalytic base might thus be one of the features responsible for the inability of the enzyme to act as a methyltransferase.
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(as it appears on PubMed at http://www.pubmed.gov), where 14607118 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14607118}}
==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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:10:16 2008''

Revision as of 01:10, 28 July 2008

Image:1qzz.png

Template:STRUCTURE 1qzz

Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)

Template:ABSTRACT PUBMED 14607118

About this Structure

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

Reference

Crystal structure of aclacinomycin-10-hydroxylase, a S-adenosyl-L-methionine-dependent methyltransferase homolog involved in anthracycline biosynthesis in Streptomyces purpurascens., Jansson A, Niemi J, Lindqvist Y, Mantsala P, Schneider G, J Mol Biol. 2003 Nov 21;334(2):269-80. PMID:14607118

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