Yun Li (@1.14) vs Crystal Pan (@5.0)
04-10-2019

Our Prediction:

Yun Li will win

Yun Li – Crystal Pan Match Prediction | 04-10-2019 04:35

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supervised the project and wrote the manuscript. C.-D.H. S.-M.L. and T.-H.L. performed the data collection and data processing. All authors participated in discussions of the results and in preparing the manuscript. J.-Y.T. and R.-L.P. assisted in protein isolation. Y.-J.S. and M.-H.L. assisted with the data collection. J.-Y.T. isolated the VrH+-PPase, grew the crystals and determined the structure. C.-L.C. assisted with structural determination and completed the structural refinement. Y.-T.H. assisted with structural phase analysis.

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Tetrazole carboxylates are acknowledged as bifunctional ligands for the construction of new coordination architectures. The X-ray diffraction results reveal that compound 1 is a linear chain in which atzpa acts as a tridentate ligand to bridge adjacent Ba2+ ions in a 1,1,3-COO mode. In contrast, compound 2 is a three-dimensional network where dtzpda4 acts as a dode-dentate ligand to bridge various Ba2+ ions. Furthermore, the luminescence of Hatzpa, H4dtzpda, compounds 1 and 2 in the solid state at room temperature were investigated. Two new coordination compounds, [Ba(atzpa)2(H2O)3]n2nH2O (1) and [Ba2(dtzpda)(H2O)]n (2) have been prepared by solvothermal reactions of BaCl22H2O with Hatzpa or H4dtzpda, respectively (Hatzpa=5-aminotetrazole-1-propanoic acid, H4dtzpda=3,3-di(1H-tetrazol-5-yl)pentanedioic acid).

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This paper reports the crystal structure of an H+-PPase in the presence of a non-hydrolysable substrate analogue. The authors propose a model for how proton pumping and pyrophosphatase hydrolysis are coupled. An unusual proton-translocation pathway is formed by six core transmembrane helices. Two types of proton-pumping protein, vacuolar H+-ATPases and H+-translocating pyrophosphatases (H+-PPases), co-exist on plant vacuolar membranes and use ATP and pyrophosphate (respectively) as energy sources for proton translocation. Whereas vacuolar H+-ATPases have been studied quite extensively, the three-dimensional structure and detailed mechanisms underlying the hydrolytic and proton-translocation reactions of H+-PPases are unclear.

A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Each VrH+-PPase subunit consists of an integral membrane domain formed by 16 transmembrane helices. We propose a working model of the mechanism for the coupling between proton pumping and PPi hydrolysis by H+-PPases. Proton pumping can be initialized by PPi hydrolysis, and H+ is then transported into the vacuolar lumen through a pathway consisting of Arg242, Asp294, Lys742 and Glu301. The three-dimensional structure and detailed mechanisms underlying the enzymatic and proton translocation reactions of H+-PPases are unclear. Here we report the crystal structure of a Vigna radiata H+-PPase (VrH+-PPase) in complex with a non-hydrolysable substrate analogue, imidodiphosphate (IDP), at 2.35 resolution. IDP is bound in the cytosolic region of each subunit and trapped by numerous charged residues and five Mg2+ ions. H+-translocating pyrophosphatases (H+-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PPi) hydrolysis1,2. H+-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes2,3.

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