3vr5 | pdb_00003vr5

Crystal structure of nucleotide-free Enterococcus hirae V1-ATPase [eV1(L)]

spinqualitylabelsall models 3vr5, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vr5 is a 8 chain structure with sequence from Atcc 8043. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 3vr2, 3vr3, 3vr4, 3vr6 Gene: ntpA (ATCC 8043), ntpB (ATCC 8043), ntpD (ATCC 8043), ntpG, ntpQ (ATCC 8043) Activity: Sodium-transporting two-sector ATPase, with EC number 3.6.3.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NTPG_ENTHA] Involved in ATP-driven sodium extrusion. [NTPA_ENTHA] Involved in ATP-driven sodium extrusion. [NTPB_ENTHA] Involved in ATP-driven sodium extrusion. Publication Abstract from PubMed In various cellular membrane systems, vacuolar ATPases (V-ATPases) function as proton pumps, which are involved in many processes such as bone resorption and cancer metastasis, and these membrane proteins represent attractive drug targets for osteoporosis and cancer. The hydrophilic V(1) portion is known as a rotary motor, in which a central axis DF complex rotates inside a hexagonally arranged catalytic A(3)B(3) complex using ATP hydrolysis energy, but the molecular mechanism is not well defined owing to a lack of high-resolution structural information. We previously reported on the in vitro expression, purification and reconstitution of Enterococcus hirae V(1)-ATPase from the A(3)B(3) and DF complexes. Here we report the asymmetric structures of the nucleotide-free (2.8 A) and nucleotide-bound (3.4 A) A(3)B(3) complex that demonstrate conformational changes induced by nucleotide binding, suggesting a binding order in the right-handed rotational orientation in a cooperative manner. The crystal structures of the nucleotide-free (2.2 A) and nucleotide-bound (2.7 A) V(1)-ATPase are also reported. The more tightly packed nucleotide-binding site seems to be induced by DF binding, and ATP hydrolysis seems to be stimulated by the approach of a conserved arginine residue. To our knowledge, these asymmetric structures represent the first high-resolution view of the rotational mechanism of V(1)-ATPase. Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures.,Arai S, Saijo S, Suzuki K, Mizutani K, Kakinuma Y, Ishizuka-Katsura Y, Ohsawa N, Terada T, Shirouzu M, Yokoyama S, Iwata S, Yamato I, Murata T Nature. 2013 Jan 31;493(7434):703-7. doi: 10.1038/nature11778. Epub 2013 Jan 13. PMID:23334411 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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