4MD2
Ground state of bacteriorhodopsin from Halobacterium salinarum
Summary for 4MD2
| Entry DOI | 10.2210/pdb4md2/pdb |
| Related | 4MD1 |
| Descriptor | Bacteriorhodopsin, 2,3-DI-PHYTANYL-GLYCEROL, (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene, ... (5 entities in total) |
| Functional Keywords | seven transmembrane helix/bacterial rhodopsins, proton pumping, membrane, transport protein, membrane protein |
| Biological source | Halobacterium sp. NRC-1 |
| Total number of polymer chains | 1 |
| Total formula weight | 39266.39 |
| Authors | Borshchevskiy, V.,Erofeev, I.,Round, E.,Weik, M.,Ishchenko, A.,Gushchin, I.,Mishin, A.,Bueldt, G.,Gordeliy, V. (deposition date: 2013-08-22, release date: 2014-10-08, Last modification date: 2024-11-27) |
| Primary citation | Borshchevskiy, V.,Round, E.,Erofeev, I.,Weik, M.,Ishchenko, A.,Gushchin, I.,Mishin, A.,Willbold, D.,Buldt, G.,Gordeliy, V. Low-dose X-ray radiation induces structural alterations in proteins. Acta Crystallogr.,Sect.D, 70:2675-2685, 2014 Cited by PubMed Abstract: X-ray-radiation-induced alterations to protein structures are still a severe problem in macromolecular crystallography. One way to avoid the influence of radiation damage is to reduce the X-ray dose absorbed by the crystal during data collection. However, here it is demonstrated using the example of the membrane protein bacteriorhodopsin (bR) that even a low dose of less than 0.06 MGy may induce structural alterations in proteins. This dose is about 500 times smaller than the experimental dose limit which should ideally not be exceeded per data set (i.e. 30 MGy) and 20 times smaller than previously detected specific radiation damage at the bR active site. To date, it is the lowest dose at which radiation modification of a protein structure has been described. Complementary use was made of high-resolution X-ray crystallography and online microspectrophotometry to quantitatively study low-dose X-ray-induced changes. It is shown that structural changes of the protein correlate with the spectroscopically observed formation of the so-called bR orange species. Evidence is provided for structural modifications taking place at the protein active site that should be taken into account in crystallographic studies which aim to elucidate the molecular mechanisms of bR function. PubMed: 25286851DOI: 10.1107/S1399004714017295 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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