1q0r

<table><tr><td colspan='2'>[[1q0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25489 Atcc 25489]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q0R FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=AKT:10-DECARBOXYMETHYLACLACINOMYCIN+T+(DCMAT)'>AKT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q0z|1q0z]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rdmc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1924 ATCC 25489])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0r OCA], [http://pdbe.org/1q0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q0r RCSB], [http://www.ebi.ac.uk/pdbsum/1q0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q0r ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RDMC_STREF RDMC_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. Catalyzes the removal of the methoxy group from the C-15 position of aclacinomycin T and A to yield 15-demethoxyaclacinomycin T and A, respectively.<ref>PMID:11004563</ref> <ref>PMID:7751313</ref>

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== Publication Abstract from PubMed ==

Aclacinomycin methylesterase (RdmC) is one of the tailoring enzymes that modify the aklavinone skeleton in the biosynthesis of anthracyclines in Streptomyces species. The crystal structures of this enzyme from Streptomyces purpurascens in complex with the product analogues 10-decarboxymethylaclacinomycin T and 10-decarboxymethylaclacinomycin A were determined to nominal resolutions of 1.45 and 1.95 A, respectively. RdmC is built up of two domains. The larger alpha/beta domain shows the common alpha/beta hydrolase fold, whereas the smaller domain is alpha-helical. The active site and substrate binding pocket are located at the interface between the two domains. Decarboxymethylaclacinomycin T and decarboxymethylaclacinomycin A bind close to the catalytic triad (Ser102-His276-Asp248) in a hydrophobic pocket, with the sugar moieties located at the surface of the enzyme. The binding of the ligands is dominated by hydrophobic interactions, and specificity appears to be controlled mainly by the shape of the binding pocket rather than through specific hydrogen bonds. Mechanistic key features consistent with the structure of complexes of RdmC with product analogues are Ser102 acting as nucleophile and transition state stabilization by an oxyanion hole formed by the backbone amides of residues Gly32 and Met103.

Crystal structure of aclacinomycin methylesterase with bound product analogues: implications for anthracycline recognition and mechanism.,Jansson A, Niemi J, Mantsala P, Schneider G J Biol Chem. 2003 Oct 3;278(40):39006-13. Epub 2003 Jul 23. PMID:12878604<ref>PMID:12878604</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1q0r" style="background-color:#fffaf0;"></div>

[[Category: Atcc 25489]]

[[Category: Jansson, A]]

[[Category: Mantsala, P]]

[[Category: Niemi, J]]

[[Category: SPINE, Structural Proteomics in Europe]]

[[Category: Schneider, G]]

[[Category: Tailoring enzyme]]