3NSB
Structure of bacteriorhodopsin ground state before and after X-ray modification
3NSB の概要
| エントリーDOI | 10.2210/pdb3nsb/pdb |
| 関連するPDBエントリー | 3NS0 |
| 分子名称 | Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | ion pump, membrane protein, retinal protein, photoreceptor, merohedral twinning, radiation damage, 7-helix transmembrane, ion transport, membrane |
| 由来する生物種 | Halobacterium salinarum (Halobacterium halobium) |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: P02945 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 32851.02 |
| 構造登録者 | |
| 主引用文献 | Borshchevskiy, V.I.,Round, E.S.,Popov, A.N.,Buldt, G.,Gordeliy, V.I. X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure. J.Mol.Biol., 409:813-825, 2011 Cited by PubMed Abstract: Bacteriorhodopsin (bR) provides light-driven vectorial proton transport across a cell membrane. Creation of electrochemical potential at the membrane is a universal step in energy transformation in a cell. Published atomic crystallographic models of early intermediate states of bR show a significant difference between them, and conclusions about pumping mechanisms have been contradictory. Here, we present a quantitative high-resolution crystallographic study of conformational changes in bR induced by X-ray absorption. It is shown that X-ray doses that are usually accumulated during data collection for intermediate-state studies are sufficient to significantly alter the structure of the protein. X-ray-induced changes occur primarily in the active site of bR. Structural modeling showed that X-ray absorption triggers retinal isomerization accompanied by the disappearance of electron densities corresponding to the water molecule W402 bound to the Schiff base. It is demonstrated that these and other X-ray-induced changes may mimic functional conformational changes of bR leading to misinterpretation of the earlier obtained X-ray crystallographic structures of photointermediates. PubMed: 21530535DOI: 10.1016/j.jmb.2011.04.038 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.78 Å) |
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