1q0r: Difference between revisions

Revision as of 03:28, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q0r.png

Template:STRUCTURE 1q0r

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)

Template:ABSTRACT PUBMED 12878604

About this StructureAbout this Structure

1Q0R is a Single protein structure of sequence from Streptomyces purpurascens. 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

Page seeded by OCA on Mon Jul 28 03:28:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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)===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12878604}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12878604 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12878604}}
 ==About this Structure==
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 [[Category: Structural proteomics in europe]]
 [[Category: Tailoring enzyme]]
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