Crystallization and preliminary crystallographic data of the PAS domain of the NifL protein from Azotobacter vinelandii.
نویسندگان
چکیده
The Azotobacter vinelandii NifL protein is a redox-sensing flavoprotein which inhibits the activity of the nitrogen-specific transcriptional activator NifA. The N-terminal PAS domain has been overexpressed in Escherichia coli and crystallized by the hanging-drop vapour-diffusion method. The crystal belongs to the rhombohedral space group R32, with unit-cell parameters a = b = 65.0, c = 157.3 A, and has one molecule in the asymmetric unit. Native data were collected to 3.0 A on the BW7B synchrotron beamline at the EMBL Hamburg Outstation.
منابع مشابه
Influence of PAS Domain Flanking Regions on Oligomerisation and Redox Signalling By NifL
Per-ARNT-Sim (PAS) domains constitute a typically dimeric, conserved α/β tertiary fold of approximately 110 amino acids that perform signalling roles in diverse proteins from all kingdoms of life. The amino terminal PAS1 domain of NifL from Azotobacter vinelandii accommodates a redox-active FAD group; elevation of cytosolic oxygen concentrations result in FAD oxidation and a concomitant conform...
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ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 57 Pt 12 شماره
صفحات -
تاریخ انتشار 2001