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1qzz

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[[Image:1qzz.jpg|left|200px]]<br /><applet load="1qzz" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qzz, resolution 2.1&Aring;" />
 
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'''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)'''<br />
 
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==Overview==
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==Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adenosyl-L-methionine (SAM)==
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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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<StructureSection load='1qzz' size='340' side='right'caption='[[1qzz]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1qzz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_purpurascens Streptomyces purpurascens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZZ FirstGlance]. <br>
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1QZZ 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=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZZ OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzz OCA], [https://pdbe.org/1qzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzz RCSB], [https://www.ebi.ac.uk/pdbsum/1qzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzz ProSAT]</span></td></tr>
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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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</table>
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[[Category: Single protein]]
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== Function ==
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[https://www.uniprot.org/uniprot/RDMB_STREF RDMB_STREF] Involved in the biosynthesis of the anthracycline aclacinomycin which is an aromatic polyketide antibiotic that exhibits high cytotoxicity and is widely applied in the chemotherapy of a variety of cancers. In vivo and in vitro, RdmB catalyzes the removal of the carboxylic group from the C-10 position of 15-demethoxyaclacinomycin T coupled to hydroxylation at the same C-10 position. It could also catalyze the removal of the carboxylic group at the C-10 position of 15-demethoxy-epsilon-rhodomycin coupled to hydroxylation at the same C-10 position to yield rhodomycin B. The reaction catalyzes by RdmB is intriguing, since the enzyme does not use any of the cofactors usually associated with hydroxylases such as flavins and/or metal ions to activate molecular oxygen.<ref>PMID:11004563</ref> <ref>PMID:15548527</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qz/1qzz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qzz ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces purpurascens]]
[[Category: Streptomyces purpurascens]]
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[[Category: Jansson, A.]]
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[[Category: Jansson A]]
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[[Category: Lindqvist, Y.]]
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[[Category: Lindqvist Y]]
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[[Category: Mantsala, P.]]
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[[Category: Mantsala P]]
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[[Category: Niemi, J.]]
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[[Category: Niemi J]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Schneider G]]
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[[Category: Schneider, G.]]
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[[Category: ACT]]
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[[Category: SAM]]
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[[Category: anthracycline]]
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[[Category: hydroxylase]]
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[[Category: methyltransferase]]
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[[Category: polyketide]]
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[[Category: spine]]
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[[Category: streptomyces]]
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[[Category: structural genomics]]
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[[Category: structural proteomics in europe]]
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[[Category: tailoring enzymes]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:36 2008''
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Current revision

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

PDB ID 1qzz

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