5fcx

Structure of Anabaena (Nostoc) sp. PCC 7120 Red Carotenoid Protein binding canthaxanthin

spinqualitylabelsall models 5fcx, resolution 3.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fcx is a 2 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 3.206Å Ligands: 45D Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8YXT8_NOSS1 Publication Abstract from PubMed Using a phylogenomic approach, we have identified and subclassified a new family of carotenoid-binding proteins. These proteins have sequence homology to the N-terminal domain (NTD) of the Orange Carotenoid Protein (OCP), and are referred to as Helical Carotenoid Proteins (HCPs). These proteins comprise at least nine distinct clades and are found in diverse organisms, frequently as multiple paralogs representing the distinct clades. These seem to be out-paralogs maintained from ancient duplications associated with subfunctionalization. All of the HCPs share conservation of the residues for carotenoid binding and we confirm that carotenoid binding is a fundamental property of HCPs. We solved two crystal structures of the Nostoc sp. PCC 7120 HCP1 protein, each binding a different carotenoid, suggesting that the proteins flexibly bind a range of carotenoids. Based on a comprehensive phylogenetic analysis, we propose that one of the HCP subtypes is likely the evolutionary ancestor of the NTD of the OCP, which arose following a domain fusion event. However, we predict that the majority of HCPs have functions distinct from the NTD of the OCP. Our results demonstrate that the HCPs are a new family of functionally diverse carotenoid-binding proteins found among ecophysiologically diverse cyanobacteria. Structure, Diversity, and Evolution of a New Family of Soluble Carotenoid Binding Proteins in Cyanobacteria.,Melnicki MR, Leverenz RL, Sutter M, Lopez-Igual R, Wilson A, Pawlowski EG, Perreau F, Kirilovsky D, Kerfeld CA Mol Plant. 2016 Jul 5. pii: S1674-2052(16)30101-0. doi:, 10.1016/j.molp.2016.06.009. PMID:27392608 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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