Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt 11):1141-3. doi: 10.1107/S1744309106042072. Epub 2006 Oct 20.

Abstract

Safety and environmental concerns have recently dictated the proper disposal of nitrilotriacetate (NTA). Biodegradation of NTA is initiated by NTA monooxygenase, which is composed of two proteins: component A and component B. The NTA monooxygenase component A protein from Corynebacterium glutamicum was crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate as the precipitant. X-ray diffraction data were collected to a maximum resolution of 2.5 A on a synchrotron beamline. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 111.04, b = 98.51, c = 171.61 A, beta = 101.94 degrees . The asymmetric unit consists of four molecules, corresponding to a packing density of 2.3 A(3) Da(-1). The structure was solved by molecular replacement. Structure refinement is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Chromatography, Gel
  • Corynebacterium / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Kinetics
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / isolation & purification
  • Mixed Function Oxygenases / metabolism
  • Molecular Weight
  • Protein Subunits / chemistry
  • Protein Subunits / isolation & purification

Substances

  • Bacterial Proteins
  • Protein Subunits
  • Mixed Function Oxygenases
  • nitrilotriacetate monooxygenase

Associated data

  • PDB/1YW1