4RVC

Structure of ATP binding subunit of ABC transporter

Summary for 4RVC

• Entry DOI: 10.2210/pdb4rvc/pdb
• Descriptor: ABC transporter ATP-binding protein (2 entities in total)
• Functional Keywords: motif c, atp bindig, transport protein
• Biological source: Geobacillus kaustophilus
• Total number of polymer chains: 1
• Total formula weight: 27554.91

Authors

Manjula, M.,Pampa, K.J.,Lokanath, N.K. (deposition date: 2014-11-26, release date: 2015-03-18, Last modification date: 2024-02-28)

Primary citation

Manjula, M.,Pampa, K.J.,Kumar, S.M.,Mukherjee, S.,Kunishima, N.,Rangappa, K.S.,Lokanath, N.K.
Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus.
Biochem.Biophys.Res.Commun., 459:113-117, 2015

PubMed 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.

PubMed: 25724946
DOI: 10.1016/j.bbrc.2015.02.079

Experimental method

X-RAY DIFFRACTION (1.77 Å)