5BN5

Structural basis for a unique ATP synthase core complex from Nanoarcheaum equitans

5BN5 の概要

• エントリーDOI: 10.2210/pdb5bn5/pdb
• 関連するPDBエントリー: 5BN3 5BN4 5BO5
• 分子名称: V-type ATP synthase alpha chain, NEQ263, SULFATE ION (3 entities in total)
• 機能のキーワード: atp synthase, nanoarcheaum equitans, catalytic core, hydrolase
• 由来する生物種: Nanoarchaeum equitans Kin4-M; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 111539.14

構造登録者

Mohanty, S.,Jobichen, C.,Chichili, V.P.R.,Sivaraman, J. (登録日: 2015-05-25, 公開日: 2015-09-16, 最終更新日: 2023-11-08)

主引用文献

Mohanty, S.,Jobichen, C.,Chichili, V.P.R.,Velazquez-Campoy, A.,Low, B.C.,Hogue, C.W.V.,Sivaraman, J.
Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans
J.Biol.Chem., 290:27280-27296, 2015

PubMed Abstract: ATP synthesis is a critical and universal life process carried out by ATP synthases. Whereas eukaryotic and prokaryotic ATP synthases are well characterized, archaeal ATP synthases are relatively poorly understood. The hyperthermophilic archaeal parasite, Nanoarcheaum equitans, lacks several subunits of the ATP synthase and is suspected to be energetically dependent on its host, Ignicoccus hospitalis. This suggests that this ATP synthase might be a rudimentary machine. Here, we report the crystal structures and biophysical studies of the regulatory subunit, NeqB, the apo-NeqAB, and NeqAB in complex with nucleotides, ADP, and adenylyl-imidodiphosphate (non-hydrolysable analog of ATP). NeqB is ∼20 amino acids shorter at its C terminus than its homologs, but this does not impede its binding with NeqA to form the complex. The heterodimeric NeqAB complex assumes a closed, rigid conformation irrespective of nucleotide binding; this differs from its homologs, which require conformational changes for catalytic activity. Thus, although N. equitans possesses an ATP synthase core A3B3 hexameric complex, it might not function as a bona fide ATP synthase.

PubMed: 26370083
DOI: 10.1074/jbc.M115.677492

実験手法

X-RAY DIFFRACTION (2.997 Å)