4md2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4md2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum_NRC-1 Halobacterium salinarum NRC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MD2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4md2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum_NRC-1 Halobacterium salinarum NRC-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MD2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SQL:(6E,10E,14E,18E)-2,6,10,15,19,23-HEXAMETHYLTETRACOSA-2,6,10,14,18,22-HEXAENE'>SQL</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SQL:(6E,10E,14E,18E)-2,6,10,15,19,23-HEXAMETHYLTETRACOSA-2,6,10,14,18,22-HEXAENE'>SQL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4md2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md2 OCA], [https://pdbe.org/4md2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4md2 RCSB], [https://www.ebi.ac.uk/pdbsum/4md2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4md2 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4md2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4md2 OCA], [https://pdbe.org/4md2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4md2 RCSB], [https://www.ebi.ac.uk/pdbsum/4md2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4md2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 19:36, 20 September 2023
Ground state of bacteriorhodopsin from Halobacterium salinarumGround state of bacteriorhodopsin from Halobacterium salinarum
Structural highlights
FunctionBACR_HALSA Light-driven proton pump. Publication Abstract from PubMedX-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. Low-dose X-ray radiation induces structural alterations in proteins.,Borshchevskiy V, Round E, Erofeev I, Weik M, Ishchenko A, Gushchin I, Mishin A, Willbold D, Buldt G, Gordeliy V Acta Crystallogr D Biol Crystallogr. 2014 Oct;70(Pt 10):2675-85. doi:, 10.1107/S1399004714017295. Epub 2014 Sep 27. PMID:25286851[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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