5bn4 | pdb_00005bn4

Structure of a unique ATP synthase NeqA-NeqB in complex with ANP from Nanoarcheaum equitans

spinqualitylabelsall models 5bn4, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bn4 is a 2 chain structure with sequence from Microarchaeum sp. kin4-m. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, MG Related: 5bn3, 5bn5, 5bo5 Gene: atpA, NEQ103 (Microarchaeum sp. Kin4-M), NEQ263 (Microarchaeum sp. Kin4-M) Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VATA_NANEQ] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. Publication Abstract from PubMed 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 structure and biophysical studies of the regulatory subunit, NeqB, the apo NeqAB, and NeqAB in complex with nucleotides, ADP and AMP-PNP. NeqB is approximately 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. Structural basis for a unique ATP synthase core complex from Nanoarcheaum Equitans.,Mohanty S, Jobichen C, Chichili VP, Velazquez-Campoy A, Low BC, Hogue CW, Sivaraman J J Biol Chem. 2015 Sep 14. pii: jbc.M115.677492. PMID:26370083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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