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Title: Structural And Functional Studies on SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase From 'Streptomyces Coelicolor' A3(2)f

Abstract

No abstract prepared.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Stanford Linear Accelerator Center (SLAC)
Sponsoring Org.:
USDOE
OSTI Identifier:
897739
Report Number(s):
SLAC-REPRINT-2006-199
TRN: US200705%%317
DOE Contract Number:
AC02-76SF00515
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochem.45:14085-14093,2006
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; FUNCTIONALS; OXIDOREDUCTASES; PROTEINS; STREPTOMYCES; Other,OTHER

Citation Formats

Tang, Y.Y., Lee, H.Y., Tang, Y., Kim, C.Y., Mathews, I., Khosla, C., and /Stanford U., Chem. Dept. /Stanford U., Chem. Eng. /SLAC, SSRL /Stanford U., Biochem. Dept. Structural And Functional Studies on SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase From 'Streptomyces Coelicolor' A3(2)f. United States: N. p., 2007. Web.
Tang, Y.Y., Lee, H.Y., Tang, Y., Kim, C.Y., Mathews, I., Khosla, C., & /Stanford U., Chem. Dept. /Stanford U., Chem. Eng. /SLAC, SSRL /Stanford U., Biochem. Dept. Structural And Functional Studies on SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase From 'Streptomyces Coelicolor' A3(2)f. United States.
Tang, Y.Y., Lee, H.Y., Tang, Y., Kim, C.Y., Mathews, I., Khosla, C., and /Stanford U., Chem. Dept. /Stanford U., Chem. Eng. /SLAC, SSRL /Stanford U., Biochem. Dept. Wed . "Structural And Functional Studies on SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase From 'Streptomyces Coelicolor' A3(2)f". United States. doi:.
@article{osti_897739,
title = {Structural And Functional Studies on SCO1815: a Beta-Ketoacyl-Acyl Carrier Protein Reductase From 'Streptomyces Coelicolor' A3(2)f},
author = {Tang, Y.Y. and Lee, H.Y. and Tang, Y. and Kim, C.Y. and Mathews, I. and Khosla, C. and /Stanford U., Chem. Dept. /Stanford U., Chem. Eng. /SLAC, SSRL /Stanford U., Biochem. Dept.},
abstractNote = {No abstract prepared.},
doi = {},
journal = {Biochem.45:14085-14093,2006},
number = ,
volume = ,
place = {United States},
year = {Wed Jan 17 00:00:00 EST 2007},
month = {Wed Jan 17 00:00:00 EST 2007}
}
  • No abstract prepared.
  • FabG from A. aeolicus, a putative component of fatty-acid synthase II, has been overexpressed, purified and crystallized. Diffraction data have been collected to 1.8 Å resolution. The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data were collected to a maximum resolution of 1.8 Å and the initial phases were determined by molecular replacement. The A. aeolicus FabG protein is a putative β-ketoacyl-acyl carrier protein reductase. Structure–function studies of this protein are being performed as partmore » of a larger project investigating naturally occurring deviations from highly conserved residues within the short-chain oxidoreductase (SCOR) family.« less
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  • The radioactively labeled {beta}-ketoacyl thioester synthase inhibitor ({sup 3}H)cerulenin was used to tag three dimeric barley chloroplast proteins ({alpha}{alpha}, {alpha}{beta}, and {beta}{beta}) from the stromal fraction. Oligonucleotides corresponding to amino acid sequences obtained from the purified proteins were used to generate with the polymerase chain reaction a probe for cDNAs encoding the {beta} subunit. cDNA sequencing revealed an open reading frame for 462 residues comprising the mature protein and a 35-amino acid transit peptide. The deduced amino acid sequence of the mature protein is homologous to the {beta}-ketoacyl-(acyl carrier protein) (ACP) synthase I (3-oxoacyl-ACP synthase; acyl-ACP:malonyl-ACP C-acyltransferase (decarboxylating), EC 2.3.1.41)more » of Escherichia coli. Under analogous experimental conditions ({sup 3}H)cerulenin tagged a single dimeric protein from spinach chloroplasts.« less