Details
| Original language | English |
|---|---|
| Pages (from-to) | 1137-1138 |
| Number of pages | 2 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 60 |
| Issue number | 6 |
| Publication status | Published - 1 Jun 2004 |
| Externally published | Yes |
Abstract
Polyketide metabolites produced by bacteria and other organisms include antibiotics, anticancer and antifungal compounds. In type II polyketide synthesis,-three enzymes are sufficient to form a polyketide product of the requisite chain length, although the fidelity of the first cyclization is variable. Addition of ketoreductase (KR) to this system results in the formation of a product with correct cyclization and reduction. This paper reports the cloning of the Streptomyces coelicolor actIII ORF5 gene that codes for the ketoreductase. The 261-amino-acid protein has been overexpressed with a 20-residue His tag, purified by affinity chromatography and crystallized in space group P3221, with unit-cell parameters a = b = 103.9, c = 123.1 Å. The crystals diffract to 2.5 A resolution. A complete data set has been collected and structure solution and refinement is under way.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
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In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 6, 01.06.2004, p. 1137-1138.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Expression, purification and preliminary X-ray diffraction analysis of a ketoreductase from a type II polyketide synthase
AU - Teartasin, Watchrra
AU - Limpkin, Claire
AU - Glod, Frank
AU - Spencer, James
AU - Cox, Russell J.
AU - Simpson, Thomas J.
AU - Crosby, John
AU - Crump, Matthew P.
AU - Hadfield, Andrea T.
PY - 2004/6/1
Y1 - 2004/6/1
N2 - Polyketide metabolites produced by bacteria and other organisms include antibiotics, anticancer and antifungal compounds. In type II polyketide synthesis,-three enzymes are sufficient to form a polyketide product of the requisite chain length, although the fidelity of the first cyclization is variable. Addition of ketoreductase (KR) to this system results in the formation of a product with correct cyclization and reduction. This paper reports the cloning of the Streptomyces coelicolor actIII ORF5 gene that codes for the ketoreductase. The 261-amino-acid protein has been overexpressed with a 20-residue His tag, purified by affinity chromatography and crystallized in space group P3221, with unit-cell parameters a = b = 103.9, c = 123.1 Å. The crystals diffract to 2.5 A resolution. A complete data set has been collected and structure solution and refinement is under way.
AB - Polyketide metabolites produced by bacteria and other organisms include antibiotics, anticancer and antifungal compounds. In type II polyketide synthesis,-three enzymes are sufficient to form a polyketide product of the requisite chain length, although the fidelity of the first cyclization is variable. Addition of ketoreductase (KR) to this system results in the formation of a product with correct cyclization and reduction. This paper reports the cloning of the Streptomyces coelicolor actIII ORF5 gene that codes for the ketoreductase. The 261-amino-acid protein has been overexpressed with a 20-residue His tag, purified by affinity chromatography and crystallized in space group P3221, with unit-cell parameters a = b = 103.9, c = 123.1 Å. The crystals diffract to 2.5 A resolution. A complete data set has been collected and structure solution and refinement is under way.
UR - http://www.scopus.com/inward/record.url?scp=4644315528&partnerID=8YFLogxK
U2 - 10.1107/S0907444904007905
DO - 10.1107/S0907444904007905
M3 - Article
C2 - 15159580
AN - SCOPUS:4644315528
VL - 60
SP - 1137
EP - 1138
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
SN - 0907-4449
IS - 6
ER -