3D31

ModBC from Methanosarcina acetivorans

3D31 の概要

• エントリーDOI: 10.2210/pdb3d31/pdb
• 分子名称: Sulfate/molybdate ABC transporter, ATP-binding protein, Sulfate/molybdate ABC transporter, permease protein, TUNGSTATE(VI)ION (3 entities in total)
• 機能のキーワード: atp-binding, nucleotide-binding, transport, membrane, transmembrane, transport protein
• 由来する生物種: Methanosarcina acetivorans; 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q8TTZ4
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143992.99

構造登録者

Gerber, S.,Comellas-Bigler, M.,Locher, K.P. (登録日: 2008-05-09, 公開日: 2008-06-10, 最終更新日: 2024-02-21)

主引用文献

Gerber, S.,Comellas-Bigler, M.,Goetz, B.A.,Locher, K.P.
Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter.
Science, 321:246-250, 2008

PubMed Abstract: Transport across cellular membranes is an essential process that is catalyzed by diverse membrane transport proteins. The turnover rates of certain transporters are inhibited by their substrates in a process termed trans-inhibition, whose structural basis is poorly understood. We present the crystal structure of a molybdate/tungstate ABC transporter (ModBC) from Methanosarcina acetivorans in a trans-inhibited state. The regulatory domains of the nucleotide-binding subunits are in close contact and provide two oxyanion binding pockets at the shared interface. By specifically binding to these pockets, molybdate or tungstate prevent adenosine triphosphatase activity and lock the transporter in an inward-facing conformation, with the catalytic motifs of the nucleotide-binding domains separated. This allosteric effect prevents the transporter from switching between the inward-facing and the outward-facing states, thus interfering with the alternating access and release mechanism.

PubMed: 18511655
DOI: 10.1126/science.1156213

実験手法

X-RAY DIFFRACTION (3 Å)