Structural highlights
Publication Abstract from PubMed
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 A 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.
Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus.,Manjula M, Pampa KJ, Kumar SM, Mukherjee S, Kunishima N, Rangappa KS, Lokanath NK Biochem Biophys Res Commun. 2015 Mar 27;459(1):113-7. doi:, 10.1016/j.bbrc.2015.02.079. Epub 2015 Feb 25. PMID:25724946[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Manjula M, Pampa KJ, Kumar SM, Mukherjee S, Kunishima N, Rangappa KS, Lokanath NK. Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus. Biochem Biophys Res Commun. 2015 Mar 27;459(1):113-7. doi:, 10.1016/j.bbrc.2015.02.079. Epub 2015 Feb 25. PMID:25724946 doi:http://dx.doi.org/10.1016/j.bbrc.2015.02.079
