1r00
From Proteopedia
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|PDB= 1r00 |SIZE=350|CAPTION= <scene name='initialview01'>1r00</scene>, resolution 2.5Å | |PDB= 1r00 |SIZE=350|CAPTION= <scene name='initialview01'>1r00</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= rdmb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1924 Streptomyces purpurascens]) | |GENE= rdmb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1924 Streptomyces purpurascens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qzz|1QZZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r00 OCA], [http://www.ebi.ac.uk/pdbsum/1r00 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r00 RCSB]</span> | ||
}} | }} | ||
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[[Category: Niemi, J.]] | [[Category: Niemi, J.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: SAH]] | ||
[[Category: anthracycline]] | [[Category: anthracycline]] | ||
[[Category: hydroxylase]] | [[Category: hydroxylase]] | ||
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[[Category: tailoring enzyme]] | [[Category: tailoring enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:18 2008'' |
Revision as of 20:21, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | rdmb (Streptomyces purpurascens) | ||||||
| Related: | 1QZZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)
Overview
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.
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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