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Literature summary for 1.1.1.100 extracted from

  • Zaccai, N.; Carter, L.; Berrow, N.; Sainsbury, S.; Nettleship, J.; Walter, T.; Harlos, K.; Owens, R.; Wilson, K.; Stuart, D.; Esnouf, R.
    Crystal structure of a 3-oxoacyl-(acyl carrier protein) reductase (BA3989) from Bacillus anthracis at 2.4 A resolution (2008), Proteins Struct. Funct. Genet., 70, 562-567.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
PCR product recombined with pDONR221 and insert from this vector transferred in the LR reaction to the expression vector pET15g which adds a histidine tag and a 3C protease cleavage site, expressed in Escherichia coli B834(DE3) cells Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment) Organism
at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis Q81JG6
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Purification (Commentary)

Purification (Comment) Organism
by nickel-affinity chromatography Bacillus anthracis

Subunits

Subunits Comment Organism
tetramer crystallography Bacillus anthracis

Synonyms

Synonyms Comment Organism
3-oxoacyl-(acyl carrier protein) reductase
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Bacillus anthracis