1. Volume 55, Issue 6, Pages 931-937 (September 2014)
Structural Biochemistry of a Vibrio cholerae Dinucleotide Cyclase Reveals Cyclase Activity Regulation by Folates 
Deyu Zhu, Lijun Wang, Guijun Shang, Xue Liu, Jing Zhu, Defen Lu, Lei Wang, Biao Kan, Jing-ren Zhang, Ye Xiang 
Molecular Cell 
Volume 55, Issue 6, Pages (September 2014)
DOI: /j.molcel
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2. Molecular Cell 2014 55, 931-937DOI: (10.1016/j.molcel.2014.08.001)
Copyright © 2014 Elsevier Inc. Terms and Conditions

3. Figure 1 Overall Structure of DncV
(A) Ribbon diagram of the DncV structure. The N and C domains are colored blue and yellow, respectively. The substrate-binding groove is indicated by a black arrow.
(B) Structural superimposition of DncV (blue) and cGAS (magenta). The substrate-binding groove is indicated by a filled arrow. The zinc finger structure of cGAS and the protruding structure of DncV are indicated by open arrows.
(C) Surface charge distribution of DncV and cGAS. Positive and negative potentials are shown in blue and red, respectively. See also Figure S1.
Molecular Cell  , DOI: ( /j.molcel )
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4. Figure 2 Structure of the Bound 5MTHFGLU2
(Left) Overall structure of the DncV-5MTHF/5MTHFGLU2-G/ATP tertiary complex showing the binding site of 5MTHF/5MTHFGLU2 and its relative position with respect to the nucleotide-binding groove. (Right) Detailed diagram showing the interaction between the bound 5MTHFGLU2 and protein residues. The carbon atoms of the bound 5MTHFGLU2 are colored green. The 2Fo–Fc density map contoured at 1.0 σ of the bound 5MTHFGLU2 is colored black. See also Figures S2 and S4.
Molecular Cell  , DOI: ( /j.molcel )
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5. Figure 3 Inhibition of DncV by 5MTHFGLU2, 5MTHF, THF, and FA
(A–D) HPLC analysis of DncV activity in the presence of inhibitors. Each measurement was performed by incubating 1 μM DncV with 1.5 mM ATP, 1.5 mM GTP, and the corresponding inhibitor at a concentration in the range of 0–4 mM for 25 min at 25°C. Arrows indicate the trends in concentration.
(E–H) Dose-response curves plotting Vi/V as a function of inhibitor concentration show the inhibition of the activities of DncV. V and Vi are the reaction velocities of DncV in the absence or presence of an inhibitor, respectively. ∗THF is unstable in solution. See also Figures S2 and S3.
Molecular Cell  , DOI: ( /j.molcel )
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6. Figure 4
Transition Structures of DncV upon Substrate Binding and Release
Structural superimpositions of DncV-di-GTP and DncV-D131A-D133A (left) and DncV-di-GTP and DncV—Δloop (right) showing the conformational changes in residues W110-Y117. Side-chain atoms of residues W110, Y117, and N116; the bound 5MTHFGLU2 and GTPs; and the Cα atoms of residues 109–119 are shown in a stick presentation with N, O, and P atoms colored blue, red, and orange, respectively. The carbon atoms of DncV-di-GTP, DncV-D131A-D133A, and DncV-Δloop are colored pink, green, and yellow, respectively.
Molecular Cell  , DOI: ( /j.molcel )
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