This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1r00
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1r00.gif|left|200px]] | [[Image:1r00.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1r00", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1r00| PDB=1r00 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''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)''' | ||
| Line 30: | Line 27: | ||
[[Category: Niemi, J.]] | [[Category: Niemi, J.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: | + | [[Category: Anthracycline]] |
| - | [[Category: | + | [[Category: Hydroxylase]] |
| - | [[Category: | + | [[Category: Methyltransferase]] |
| - | [[Category: | + | [[Category: Polyketide]] |
| - | [[Category: | + | [[Category: Streptomyce]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 03:54, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:54:38 2008
