Purification and X-ray crystallographic analysis of 7-keto-8-aminopelargonic acid (KAPA) synthase from Mycobacterium smegmatis

Shanghua Fan, Defeng Li, Joy Fleming, Yuan Hong, Tao Chen, Lin Zhou, Lijun Bi, Dacheng Wang, Xianen Zhang, Guanjun Chen

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

7-Keto-8-aminopelargonic acid synthase (KAPA synthase; BioF) is an essential enzyme for mycobacterial growth that catalyses the first committed step in the biotin-synthesis pathway. It is a pyridoxal 5′-phosphate (PLP)-dependent enzyme and is a potential drug target. Here, the cloning, expression, purification and crystallization of KAPA synthase from Mycobacterium smegmatis (MsBioF) and the characterization of MsBioF crystals using X-ray diffraction are described. The crystals diffracted to 2.3 Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 70.88, b = 91.68, c = 109.84 Å, β = 97.8°. According to the molecular weight of MsBioF, the unit-cell parameters and the self-rotation function map, four molecules are present in each asymmetric unit with a V M value of 2.06 Å3 Da-1 and a solvent content of 40.20%.

Original languageEnglish (US)
Pages (from-to)1372-1375
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
DOIs
StatePublished - Jan 1 2014
Externally publishedYes

Keywords

  • 7-keto-8-aminopelargonic acid (KAPA) synthase
  • biotin-synthesis pathway
  • Mycobacterium smegmatis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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