6s5l

Anabaena Apo-C-Terminal Domain Homolog Of The Orange Carotenoid Protein In Native Conditions

spinqualitylabelsall models 6s5l, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6s5l is a 12 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YMJ3_NOSS1 Publication Abstract from PubMed The structural features enabling carotenoid translocation between molecular entities in nature is poorly understood. Here, we present the three-dimensional X-ray structure of an expanded oligomeric state of the C-terminal domain homolog (CTDH) of the orange carotenoid protein, a key water-soluble protein in cyanobacterial photosynthetic photo-protection, at 2.9A resolution. This protein binds a canthaxanthin carotenoid ligand and undergoes structural reorganization at the dimeric level, which facilitates cargo uptake and delivery. The structure displays heterogeneity revealing the dynamic nature of its C-terminal tail (CTT). Molecular dynamics (MD) simulations based on the CTDH structures identified specific residues that govern the dimeric transition mechanism. Mutagenesis based on the crystal structure and these MD simulations then confirmed that these specific residues within the CTT are critical for carotenoid uptake, encapsulation and delivery processes. We present a mechanism that can be applied to other systems that require cargo uptake. Structural dynamics in the C terminal domain homolog of orange carotenoid protein reveals residues critical for carotenoid uptake.,Harris D, Muzzopappa F, Glaser F, Wilson A, Kirilovsky D, Adir N Biochim Biophys Acta Bioenerg. 2020 Apr 29:148214. doi:, 10.1016/j.bbabio.2020.148214. PMID:32360310 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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