1q0r: Difference between revisions
New page: left|200px<br /><applet load="1q0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q0r, resolution 1.45Å" /> '''Crystal structure of... |
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[[Image:1q0r.jpg|left|200px]]<br /><applet load="1q0r" size=" | [[Image:1q0r.jpg|left|200px]]<br /><applet load="1q0r" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1q0r, resolution 1.45Å" /> | caption="1q0r, resolution 1.45Å" /> | ||
'''Crystal structure of aclacinomycin methylesterase (RdmC) with bound product analogue, 10-decarboxymethylaclacinomycin T (DcmaT)'''<br /> | '''Crystal structure of aclacinomycin methylesterase (RdmC) with bound product analogue, 10-decarboxymethylaclacinomycin T (DcmaT)'''<br /> | ||
==Overview== | ==Overview== | ||
Aclacinomycin methylesterase (RdmC) is one of the tailoring enzymes that | 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. | ||
==About this Structure== | ==About this Structure== | ||
1Q0R 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 AKT, SO4 and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1Q0R 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=AKT:'>AKT</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0R OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mantsala, P.]] | [[Category: Mantsala, P.]] | ||
[[Category: Niemi, J.]] | [[Category: Niemi, J.]] | ||
[[Category: SPINE, Structural | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
[[Category: 1PE]] | [[Category: 1PE]] | ||
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[[Category: tailoring enzyme]] | [[Category: tailoring enzyme]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:39 2008'' | ||
Revision as of 15:34, 21 February 2008
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Crystal structure of aclacinomycin methylesterase (RdmC) with bound product analogue, 10-decarboxymethylaclacinomycin T (DcmaT)
OverviewOverview
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.
About this StructureAbout this Structure
1Q0R is a Single protein structure of sequence from Streptomyces purpurascens with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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