5BN5
Structural basis for a unique ATP synthase core complex from Nanoarcheaum equitans
Summary for 5BN5
| Entry DOI | 10.2210/pdb5bn5/pdb |
| Related | 5BN3 5BN4 5BO5 |
| Descriptor | V-type ATP synthase alpha chain, NEQ263, SULFATE ION (3 entities in total) |
| Functional Keywords | atp synthase, nanoarcheaum equitans, catalytic core, hydrolase |
| Biological source | Nanoarchaeum equitans Kin4-M More |
| Total number of polymer chains | 2 |
| Total formula weight | 111539.14 |
| Authors | Mohanty, S.,Jobichen, C.,Chichili, V.P.R.,Sivaraman, J. (deposition date: 2015-05-25, release date: 2015-09-16, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 26370083DOI: 10.1074/jbc.M115.677492 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.997 Å) |
Structure validation
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