1GAJ

CRYSTAL STRUCTURE OF A NUCLEOTIDE-FREE ATP-BINDING CASSETTE FROM AN ABC TRANSPORTER

Summary for 1GAJ

• Entry DOI: 10.2210/pdb1gaj/pdb
• Related: 1g6h
• Descriptor: HIGH-AFFINITY BRANCHED CHAIN AMINO ACID TRANSPORT ATP-BINDING PROTEIN, SULFATE ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: abc transporter, active transport, atpase, nucleotide-binding domain, transport protein
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 1
• Total formula weight: 29630.26

Authors

Karpowich, N.,Yuan, Y.-R.,Dai, P.L.,Martsinkevich, O.,Millen, L.,Thomas, P.J.,Hunt, J.F. (deposition date: 2000-11-30, release date: 2001-07-18, Last modification date: 2024-02-07)

Primary citation

Karpowich, N.,Martsinkevich, O.,Millen, L.,Yuan, Y.R.,Dai, P.L.,MacVey, K.,Thomas, P.J.,Hunt, J.F.
Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter.
Structure, 9:571-586, 2001

PubMed Abstract: ATP binding cassette (ABC) transporters are ubiquitously distributed transmembrane solute pumps that play a causative role in numerous diseases. Previous structures have defined the fold of the ABC and established the flexibility of its alpha-helical subdomain. But the nature of the mechanical changes that occur at each step of the chemical ATPase cycle have not been defined.

PubMed: 11470432
DOI: 10.1016/S0969-2126(01)00617-7

Experimental method

X-RAY DIFFRACTION (2.5 Å)