5ze9 | pdb_00005ze9

Crystal structure of AMP-PNP bound mutant A3B3 complex from Enterococcus hirae V-ATPase

spinqualitylabelsall models 5ze9, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ze9 is a 6 chain structure with sequence from Entha. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ANP, GOL, MES, MG Gene: ntpA, EHR_08260 (ENTHA), ntpB, EHR_08265 (ENTHA) Activity: Sodium-transporting two-sector ATPase, with EC number 3.6.3.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NTPA_ENTHA] Involved in ATP-driven sodium extrusion. [NTPB_ENTHA] Involved in ATP-driven sodium extrusion. Publication Abstract from PubMed V1-ATPase is an ATP-driven rotary motor that is composed of a ring-shaped A3B3 complex and a central DF shaft. The nucleotide-free A3B3 complex of Enterococcus hirae, composed of three identical A1B1 heterodimers, showed a unique asymmetrical structure, probably due to the strong binding of the N-terminal barrel domain, which forms a crown structure. Here, we mutated the barrel region to weaken the crown, and performed structural analyses using high-speed atomic force microscopy and x-ray crystallography of the mutant A3B3. The nucleotide-free mutant A3B3 complex had a more symmetrical open structure than the wild type. Binding of nucleotides produced a closely packed spiral-like structure with a disrupted crown. These findings suggest that wild-type A3B3 forms a metastable (stressed) asymmetric structure composed of unstable A1B1 conformers due to the strong constraint of the crown. The results further the understanding of the principle of the cooperative transition mechanism of rotary motors. Metastable asymmetrical structure of a shaftless V1 motor.,Maruyama S, Suzuki K, Imamura M, Sasaki H, Matsunami H, Mizutani K, Saito Y, Imai FL, Ishizuka-Katsura Y, Kimura-Someya T, Shirouzu M, Uchihashi T, Ando T, Yamato I, Murata T Sci Adv. 2019 Jan 30;5(1):eaau8149. doi: 10.1126/sciadv.aau8149. eCollection 2019, Jan. PMID:30729160 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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