1r00

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[[Image:1r00.gif|left|200px]]<br /><applet load="1r00" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r00.gif|left|200px]]
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caption="1r00, resolution 2.5&Aring;" />
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'''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)'''<br />
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{{Structure
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|PDB= 1r00 |SIZE=350|CAPTION= <scene name='initialview01'>1r00</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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|ACTIVITY=
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|GENE= rdmb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1924 Streptomyces purpurascens])
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}}
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'''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-homocystein (SAH)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1R00 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R00 OCA].
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1R00 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R00 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14607118 14607118]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14607118 14607118]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces purpurascens]]
[[Category: Streptomyces purpurascens]]
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[[Category: methyltransferase]]
[[Category: methyltransferase]]
[[Category: polyketide]]
[[Category: polyketide]]
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[[Category: streptomyces]]
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[[Category: streptomyce]]
[[Category: tailoring enzyme]]
[[Category: tailoring enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:00 2008''

Revision as of 11:45, 20 March 2008


PDB ID 1r00

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: and
Gene: rdmb (Streptomyces purpurascens)
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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