Table 1.
X-ray data collection and refinement table.
Fig 1.
(A) Cartoon representation of a crystallographic asymmetric unit containing two copies of the MBP-PYD fusion protein. The MBPs are colored in grey, and the PYDs in chains A and B, are colored in green and cyan, respectively. (B) MBP-PYD structure in chain A. The amino terminus is labeled by “N” and the Carboxyl terminus is labeled by “C”. The linker region is colored in wheat and shown in sticks. The maltose molecule bound to MBP is shown in spheres.
Fig 2.
Structural comparison of chain A and chain B.
(A) Superposition of chain A and chain B. The MBP regions of the two chains were aligned. (B) Structure of the NLRP12 PYD domain. A. The 6 helices are labeled as H1-H6. (C) Superposition of PYD domain in chain A and chain B.
Fig 3.
Structural comparison with other NLRP PYD domains.
The PYD structures of NLRP1 (PDB: 1PN5, color: teal), NLRP3 (PDB: 3QF2, color: violet), NLRP7 (PDB: 2KM6, color: wheat) and NLRP10 (PDB: 2DO9, color: orange) were superimposed onto our NLRP12 PYD chain A.
Fig 4.
Disulfide bond-mediated dimerization.
(A) The disulfide bond is formed between the Cys11 residues from chain A and chain B. It is colored in gold. (B) Sequence alignment of the PYD region of selected NLRP12 and NLRP3 proteins. The helices were labeled as H1- H6. The conserved region are colored with yellow background. The conserved cysteine residues are indicated with a purple triangle. (C) Intra-molecular disulfide bond of human NLRP3 PYD. An intra-molecular disulfide bond between Cys8 and Cys108 was observed in the reported crystal structure of the human NLRP3 PYD (PDB: 3QF2).