Journal article
NikD, an Unusual Amino Acid Oxidase Essential for Nikkomycin Biosynthesis: Structures of Closed and Open Forms at 1.15 and 1.90 Å Resolution
Structure (London), v 15(8), pp 928-941
2007
PMID: 17697998
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
NikD is an unusual amino-acid-oxidizing enzyme that contains covalently bound FAD, catalyzes a 4-electron oxidation of piperideine-2-carboxylic acid to picolinate, and plays a critical role in the biosynthesis of nikkomycin antibiotics. Crystal structures of closed and open forms of nikD, a two-domain enzyme, have been determined to resolutions of 1.15 and 1.9 Å, respectively. The two forms differ by an 11° rotation of the catalytic domain with respect to the FAD-binding domain. The active site is inaccessible to solvent in the closed form; an endogenous ligand, believed to be picolinate, is bound close to and parallel with the flavin ring, an orientation compatible with redox catalysis. The active site is solvent accessible in the open form, but the picolinate ligand is approximately perpendicular to the flavin ring and a tryptophan is stacked above the flavin ring. NikD also contains a mobile cation binding loop.
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Details
- Title
- NikD, an Unusual Amino Acid Oxidase Essential for Nikkomycin Biosynthesis: Structures of Closed and Open Forms at 1.15 and 1.90 Å Resolution
- Creators
- Christopher J Carrell - Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USARobert C Bruckner - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USADavid Venci - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USAGouhua Zhao - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USAMarilyn Schuman Jorns - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USAF. Scott Mathews - Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110, USA
- Publication Details
- Structure (London), v 15(8), pp 928-941
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000248822200008
- Scopus ID
- 2-s2.0-34547663087
- Other Identifier
- 991014877799104721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics
- Cell Biology