3CNI

Crystal structure of a domain of a putative ABC type-2 transporter from Thermotoga maritima MSB8

3CNI の概要

• エントリーDOI: 10.2210/pdb3cni/pdb
• 分子名称: Putative ABC type-2 transporter, CALCIUM ION (3 entities in total)
• 機能のキーワード: structural genomics, abc type-2 transporter, thermotoga maritima, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, transport protein
• 由来する生物種: Thermotoga maritima MSB8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17217.44

構造登録者

Filippova, E.V.,Shumilin, I.,Tkaczuk, K.L.,Cymborowski, M.,Chruszcz, M.,Xu, X.,Que, Q.,Savchenko, A.,Edwards, A.M.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (登録日: 2008-03-25, 公開日: 2008-04-08, 最終更新日: 2024-11-13)

主引用文献

Filippova, E.V.,Tkaczuk, K.L.,Chruszcz, M.,Xu, X.,Savchenko, A.,Edwards, A.,Minor, W.
Structural characterization of the putative ABC-type 2 transporter from Thermotoga maritima MSB8.
J.Struct.Funct.Genom., 15:215-222, 2014

PubMed Abstract: This study describes the structure of the putative ABC-type 2 transporter TM0543 from Thermotoga maritima MSB8 determined at a resolution of 2.3 Å. In comparative sequence-clustering analysis, TM0543 displays similarity to NatAB-like proteins, which are components of the ABC-type Na(+) efflux pump permease. However, the overall structure fold of the predicted nucleotide-binding domain reveals that it is different from any known structure of ABC-type efflux transporters solved to date. The structure of the putative TM0543 domain also exhibits different dimer architecture and topology of its presumed ATP binding pocket, which may indicate that it does not bind nucleotide at all. Structural analysis of calcium ion binding sites found at the interface between TM0543 dimer subunits suggests that protein may be involved in ion-transporting activity. A detailed analysis of the protein sequence and structure is presented and discussed.

PubMed: 25306867
DOI: 10.1007/s10969-014-9189-7

実験手法

X-RAY DIFFRACTION (2.3 Å)