Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus

Biochemical and Biophysical Research Communications
M ManjulaN K Lokanath

Abstract

The ATP binding cassette (ABC) transporters, represent one of the largest superfamilies of primary transporters, which are very essential for various biological functions. The crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus has been determined at 1.77 Å resolution. The crystal structure revealed that the protomer has two thick arms, (arm I and II), which resemble 'L' shape. The ATP-binding pocket is located close to the end of arm I. ATP molecule is docked into the active site of the protein. The dimeric crystal structure of ATP-binding subunit of ABC transporter from G. kaustophilus has been compared with the previously reported crystal structure of ATP-binding subunit of ABC transporter from Salmonella typhimurium.

References

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Nov 13, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Mallappa ManjulaNeratur K Lokanath

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