1L7V

Bacterial ABC Transporter Involved in B12 Uptake

1L7V の概要

• エントリーDOI: 10.2210/pdb1l7v/pdb
• 分子名称: VITAMIN B12 TRANSPORT SYSTEM PERMEASE PROTEIN BTUC, Vitamin B12 transport ATP-binding protein btuD, CYCLO-TETRAMETAVANADATE (3 entities in total)
• 機能のキーワード: abc transporter, integral membrane protein, atp binding cassette, atp hydrolysis, vitamin b12, transport protein-hydrolase complex, transport protein/hydrolase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P06609; Cell inner membrane; Peripheral membrane protein: P06611
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 126839.87

構造登録者

Locher, K.P.,Lee, A.T.,Rees, D.C. (登録日: 2002-03-18, 公開日: 2002-05-15, 最終更新日: 2024-11-20)

主引用文献

Locher, K.P.,Lee, A.T.,Rees, D.C.
The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism.
Science, 296:1091-1098, 2002

PubMed Abstract: The ABC transporters are ubiquitous membrane proteins that couple adenosine triphosphate (ATP) hydrolysis to the translocation of diverse substrates across cell membranes. Clinically relevant examples are associated with cystic fibrosis and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we report the crystal structure at 3.2 angstrom resolution of the Escherichia coli BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and appears to represent a conserved motif among the ABC transporters.

PubMed: 12004122
DOI: 10.1126/science.1071142

実験手法

X-RAY DIFFRACTION (3.2 Å)