4U02

Crystal structure of apo-TTHA1159

4U02 の概要

• エントリーDOI: 10.2210/pdb4u02/pdb
• 関連するPDBエントリー: 4U00
• 分子名称: Amino acid ABC transporter, ATP-binding protein, SULFATE ION (3 entities in total)
• 機能のキーワード: atp binding protein, abc amino acid transporter, nucleotide binding domain, transport protein
• 由来する生物種: Thermus thermophilus HB8
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 111705.92

構造登録者

Karthiga Devi, S.,Chichili, V.P.R.,Velmurugan, D.,Sivaraman, J. (登録日: 2014-07-11, 公開日: 2015-05-13, 最終更新日: 2024-03-20)

主引用文献

Devi, S.K.,Chichili, V.P.,Jeyakanthan, J.,Velmurugan, D.,Sivaraman, J.
Structural basis for the hydrolysis of ATP by a nucleotide binding subunit of an amino acid ABC transporter from Thermus thermophilus
J.Struct.Biol., 190:367-372, 2015

PubMed Abstract: ATP-binding cassette (ABC) transporters are a major family of small molecule transporter proteins, and their deregulation is associated with several diseases, including cancer. Here, we report the crystal structure of the nucleotide binding domain (NBD) of an amino acid ABC transporter from Thermus thermophilus (TTHA1159) in its apo form and as a complex with ADP along with functional studies. TTHA1159 is a putative arginine ABC transporter. The apo-TTHA1159 was crystallized in dimeric form, a hitherto unreported form of an apo NBD. Structural comparison of the apo and ADP-Mg(2+) complexes revealed that Phe14 of TTHA1159 undergoes a significant conformational change to accommodate ADP, and that the bound ADP interacts with the P-loop (Gly40-Thr45). Modeling of ATP-Mg(2+):TTHA1159 complex revealed that Gln86 and Glu164 are involved in water-mediated hydrogen bonding contacts and Asp163 in Mg(2+) ion-mediated hydrogen bonding contacts with the γ-phosphate of ATP, consistent with the findings of other ABC transporters. Mutational studies confirmed the necessity of each of these residues, and a comparison of the apo/ADP Mg(2+):TTHA1159 with its ATP-complex model suggests the likelihood of a key conformational change to the Gln86 side chain for ATP hydrolysis.

PubMed: 25916755
DOI: 10.1016/j.jsb.2015.04.012

実験手法

X-RAY DIFFRACTION (2.399 Å)