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| - | [[Image:1r00.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1r00.png|left|200px]] |
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| | {{STRUCTURE_1r00| PDB=1r00 | SCENE= }} | | {{STRUCTURE_1r00| PDB=1r00 | SCENE= }} |
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| - | '''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)'''
| + | ===Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)=== |
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14607118}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14607118 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14607118}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Streptomyce]] | | [[Category: Streptomyce]] |
| | [[Category: Tailoring enzyme]] | | [[Category: Tailoring enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:54:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:59:05 2008'' |
Revision as of 18:59, 27 July 2008
Template:STRUCTURE 1r00
Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)
Template:ABSTRACT PUBMED 14607118
About this Structure
1R00 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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