6rf4 | pdb_00006rf4

Crystal structure of the potassium-pumping S254A mutant of the light-driven sodium pump KR2 in the pentameric form, pH 8.0

spinqualitylabelsall models 6rf4, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rf4 is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG, LFA, NA, OLC, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Rhodopsins are the most universal biological light-energy transducers and abundant phototrophic mechanisms that evolved on Earth and have a remarkable diversity and potential for biotechnological applications. Recently, the first sodium-pumping rhodopsin KR2 from Krokinobacter eikastus was discovered and characterized. However, the existing structures of KR2 are contradictory, and the mechanism of Na(+) pumping is not yet understood. Here, we present a structure of the cationic (non H(+)) light-driven pump at physiological pH in its pentameric form. We also present 13 atomic structures and functional data on the KR2 and its mutants, including potassium pumps, which show that oligomerization of the microbial rhodopsin is obligatory for its biological function. The studies reveal the structure of KR2 at nonphysiological low pH where it acts as a proton pump. The structure provides new insights into the mechanisms of microbial rhodopsins and opens the way to a rational design of novel cation pumps for optogenetics. Structure and mechanisms of sodium-pumping KR2 rhodopsin.,Kovalev K, Polovinkin V, Gushchin I, Alekseev A, Shevchenko V, Borshchevskiy V, Astashkin R, Balandin T, Bratanov D, Vaganova S, Popov A, Chupin V, Buldt G, Bamberg E, Gordeliy V Sci Adv. 2019 Apr 10;5(4):eaav2671. doi: 10.1126/sciadv.aav2671. eCollection 2019, Apr. PMID:30989112 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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