8dn7

The crystal structure of the Pisum sativum Toc75 POTRA domains in complex with fab ax9

spinqualitylabelsall models 8dn7, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8dn7 is a 6 chain structure with sequence from Pisum sativum and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TOC75_PEA Mediates the insertion of proteins targeted to the outer membrane of chloroplasts. Required for the import of protein precursors into chloroplasts. Forms the voltage-dependent preprotein translocation channels (hydrophilic beta barrel) of the TOC complex in the chloroplastic outer membrane. The narrowest inner diameter of this channel is approximately 14 Angstroms. Publication Abstract from PubMed Roughly 95% of the proteins that make up the chloroplast must be imported from the cytoplasm. The machinery responsible for the translocation of these cargo proteins is called the translocon at the outer membrane of chloroplast (TOC). The TOC core consists of three proteins, Toc34, Toc75, and Toc159; no high-resolution structure has been solved of fully assembled TOC from plants. Efforts toward determining the structure of the TOC have been hindered almost entirely by difficulties in producing sufficient yields for structural studies. In this study, we introduce an innovative method that utilizes synthetic antigen binding fragments (sABs) to isolate TOC directly from wild-type plant biomass including A. thaliana and P. sativum. Binding between the sABs and the POTRA domains was characterized by size-exclusion chromatography coupled with small-angle X-ray scattering (SEC-SAXS), X-ray crystallography, and isothermal titration calorimetry. We also demonstrate the isolation of the TOC from P. sativum, laying the framework for large-scale isolation and purification of TOC for functional and structural studies. Characterization of synthetic antigen binding fragments targeting Toc75 for the isolation of TOC in A. thaliana and P. sativum.,Srinivasan K, Erramilli SK, Chakravarthy S, Gonzalez A, Kossiakoff A, Noinaj N Structure. 2023 May 4;31(5):595-606.e5. doi: 10.1016/j.str.2023.03.002. Epub 2023 , Mar 27. PMID:36977410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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