1q0r: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1q0r]] is a 1 chain structure with 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=1Q0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0R FirstGlance]. <br> | <table><tr><td colspan='2'>[[1q0r]] is a 1 chain structure with 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=1Q0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0R FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0z|1q0z]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0z|1q0z]]</td></tr> | ||
<tr><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 Streptomyces purpurascens])</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 Streptomyces purpurascens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q0r RCSB], [http://www.ebi.ac.uk/pdbsum/1q0r PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q0r RCSB], [http://www.ebi.ac.uk/pdbsum/1q0r PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q54528_9ACTO Q54528_9ACTO]] 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:7751313</ref> <ref>PMID:11004563</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Streptomyces purpurascens]] | [[Category: Streptomyces purpurascens]] | ||
[[Category: Jansson, A | [[Category: Jansson, A]] | ||
[[Category: Mantsala, P | [[Category: Mantsala, P]] | ||
[[Category: Niemi, J | [[Category: Niemi, J]] | ||
[[Category: SPINE, Structural Proteomics in Europe | [[Category: SPINE, Structural Proteomics in Europe]] | ||
[[Category: Schneider, G | [[Category: Schneider, G]] | ||
[[Category: Anthracycline]] | [[Category: Anthracycline]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 02:39, 25 December 2014
Crystal structure of aclacinomycin methylesterase (RdmC) with bound product analogue, 10-decarboxymethylaclacinomycin T (DcmaT)Crystal structure of aclacinomycin methylesterase (RdmC) with bound product analogue, 10-decarboxymethylaclacinomycin T (DcmaT)
Structural highlights
Function[Q54528_9ACTO] 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.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAclacinomycin 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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