5wtp | pdb_00005wtp

Crystal structure of the C-terminal domain of outer membrane protein A (OmpA) from Capnocytophaga gingivalis

spinqualitylabelsall models 5wtp, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wtp is a 3 chain structure with sequence from Capnocytophaga gingivalis ATCC 33624. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C2M2E7_CAPGI Publication Abstract from PubMed Eukaryotic thrombospondin type 3 repeat (TT3R) is an efficient calcium ion (Ca(2+)) binding motif only found in mammalian thrombospondin family. TT3R has also been found in prokaryotic cellulase Cel5G, which was thought to forfeit the Ca(2+)-binding capability due to the formation of intra-repeat disulfide bonds, instead of the inter-repeat ones possessed by eukaryotic TT3Rs. In this study, we have identified an enormous number of prokaryotic TT3R-containing proteins belonging to several different protein families, including outer membrane protein A (OmpA), an important structural protein connecting the outer membrane and the periplasmic peptidoglycan layer in gram-negative bacteria. Here, we report the crystal structure of the periplasmic region of OmpA from Capnocytophaga gingivalis, which contains a linker region comprising five consecutive TT3Rs. The structure of OmpA-TT3R exhibits a well-ordered architecture organized around two tightly-coordinated Ca(2+) and confirms the presence of abnormal intra-repeat disulfide bonds. Further mutagenesis studies showed that the Ca(2+)-binding capability of OmpA-TT3R is indeed dependent on the proper formation of intra-repeat disulfide bonds, which help to fix a conserved glycine residue at its proper position for Ca(2+) coordination. Additionally, despite lacking inter-repeat disulfide bonds, the interfaces between adjacent OmpA-TT3Rs are enhanced by both hydrophobic and conserved aromatic-proline interactions. Structure of thrombospondin type 3 repeats in bacterial outer membrane protein A reveals its intra-repeat disulfide bond-dependent calcium-binding capability.,Dai S, Sun C, Tan K, Ye S, Zhang R Cell Calcium. 2017 Sep;66:78-89. doi: 10.1016/j.ceca.2017.05.016. Epub 2017 Jun, 9. PMID:28807152 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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