<p>Shown is the overall fold of VldE as well as comparison to OtsA by superimposition. (<b>A</b>) The overall fold of the monomeric VldE is represented in a ribbon diagram. The monomer is rendered with the N-terminal domain in red, and the C-terminal domain in blue. The α-helical C-terminus, which stretches back across both domains, is rendered in green. VldE consists of twin Rossman-like β/α/β domains in a GT-B configuration with the catalytic site marked by VDO and GDP at the interface of the two domains. (<b>B</b>) To compare the overall fold of VldE (green) to OtsA (gray), the folding patterns, which were represented by a tracing of C<sup>α</sup>, were superimposed. (<b>C</b>) Shown is a topology diagram of VldE with β-strands and α-hel...
<p>Schematic depiction of the progression of folding for WT IL-1β, (far left) PM23 (center left), PM...
<p>Ribbon diagram representations of the 3D structures of UmpH (PDB id: 2c4n) and YutF (PDB id: 3pdw...
<p>A) Plot of number of residue correspondences vs. RMSD in each structure (d1gt8a4 is in green, d1m...
<p>Shown is a comparison of the VldE and OtsA catalytic sites in ribbon diagrams. Residues/molecules...
<p>Shown are ribbon diagrams of the three conformers of VldE modeled using the VldE·GDP·TRE crystall...
<p>A. Surface and cartoon representation of BvgS showing that VFT1-B is open and VFT2-A is in an apo...
<p>The Rossmann is a β/α fold, namely a consecutive repeat of motifs comprising a β-strand (in yello...
<p>(a) Ribbon diagram overlap. The ribbon diagram of OtsA (colored in blue) is superposed with that ...
<p>Topology diagram of UGT from <i>F. ananassa</i> shows CTD and NTD having an architecture of Rossm...
<p>A) The TLP protomer is divided into two domains. The N-terminal thiolase domain can further be di...
<p>Nine representatives of the selected vRdPs were chosen. Their structures are shown as a ribbon di...
<p>The α-helices and β-strands of three domains are colored with different colors (upper). The catal...
<p>A. Surface representation of protomer B (in blue); the residues interacting with protomer A are s...
<p>Side by side comparison of the VP1 structures from the native virion (A) and the 80S particle (B)...
<p>A. Schematic representation of the homodimeric BvgS periplasmic portion. The protomers A and B ar...
<p>Schematic depiction of the progression of folding for WT IL-1β, (far left) PM23 (center left), PM...
<p>Ribbon diagram representations of the 3D structures of UmpH (PDB id: 2c4n) and YutF (PDB id: 3pdw...
<p>A) Plot of number of residue correspondences vs. RMSD in each structure (d1gt8a4 is in green, d1m...
<p>Shown is a comparison of the VldE and OtsA catalytic sites in ribbon diagrams. Residues/molecules...
<p>Shown are ribbon diagrams of the three conformers of VldE modeled using the VldE·GDP·TRE crystall...
<p>A. Surface and cartoon representation of BvgS showing that VFT1-B is open and VFT2-A is in an apo...
<p>The Rossmann is a β/α fold, namely a consecutive repeat of motifs comprising a β-strand (in yello...
<p>(a) Ribbon diagram overlap. The ribbon diagram of OtsA (colored in blue) is superposed with that ...
<p>Topology diagram of UGT from <i>F. ananassa</i> shows CTD and NTD having an architecture of Rossm...
<p>A) The TLP protomer is divided into two domains. The N-terminal thiolase domain can further be di...
<p>Nine representatives of the selected vRdPs were chosen. Their structures are shown as a ribbon di...
<p>The α-helices and β-strands of three domains are colored with different colors (upper). The catal...
<p>A. Surface representation of protomer B (in blue); the residues interacting with protomer A are s...
<p>Side by side comparison of the VP1 structures from the native virion (A) and the 80S particle (B)...
<p>A. Schematic representation of the homodimeric BvgS periplasmic portion. The protomers A and B ar...
<p>Schematic depiction of the progression of folding for WT IL-1β, (far left) PM23 (center left), PM...
<p>Ribbon diagram representations of the 3D structures of UmpH (PDB id: 2c4n) and YutF (PDB id: 3pdw...
<p>A) Plot of number of residue correspondences vs. RMSD in each structure (d1gt8a4 is in green, d1m...