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5BN5

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

Summary for 5BN5
Entry DOI10.2210/pdb5bn5/pdb
Related5BN3 5BN4 5BO5
DescriptorV-type ATP synthase alpha chain, NEQ263, SULFATE ION (3 entities in total)
Functional Keywordsatp synthase, nanoarcheaum equitans, catalytic core, hydrolase
Biological sourceNanoarchaeum equitans Kin4-M
More
Total number of polymer chains2
Total formula weight111539.14
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 citationMohanty, 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: 26370083
DOI: 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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数据于2024-11-06公开中

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