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

Manjula, M. and Pampa, K. J. and Kumar, S. M. and Mukherjee, S. and Kunishima, N. and Rangappa, K. S. and Lokanath, N. K. (2015) Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 459 (1). pp. 113-117. ISSN 1090-2104

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Official URL: https://doi.org/10.1016/j.bbrc.2015.02.079

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 angstrom 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 Geobacillus kaustophilus has been compared with the previously reported crystal structure of ATP-binding subunit of ABC transporter from Salmonella typhimurium. (C) 2015 Elsevier Inc. All rights reserved.

Item Type: Article
Subjects: B Life Science > Microbiology
C Chemical Science > Chemistry
D Physical Science > Physics
Divisions: Department of > Chemistry
Department of > Microbiology
Department of > Physics
Depositing User: Shrirekha N
Date Deposited: 13 Jun 2019 10:25
Last Modified: 13 Jun 2019 10:25
URI: http://eprints.uni-mysore.ac.in/id/eprint/2774

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