|  |  | 
		| Line 3: | Line 3: | 
|  | <StructureSection load='3lsa' size='340' side='right'caption='[[3lsa]], [[Resolution|resolution]] 1.79Å' scene=''> |  | <StructureSection load='3lsa' size='340' side='right'caption='[[3lsa]], [[Resolution|resolution]] 1.79Å' scene=''> | 
|  | == Structural highlights == |  | == Structural highlights == | 
| - | <table><tr><td colspan='2'>[[3lsa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pectiniidae Pectiniidae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LSA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lsa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectiniidae Pectiniidae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LSA FirstGlance]. <br> | 
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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]] 1.79Å</td></tr> | 
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYC:[(4Z)-2-[(1R)-1-AMINO-2-MERCAPTOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYC</scene></td></tr>
 | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GYC:[(4Z)-2-[(1R)-1-AMINO-2-MERCAPTOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr> | 
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ls3|3ls3]]</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=3lsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsa OCA], [https://pdbe.org/3lsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lsa RCSB], [https://www.ebi.ac.uk/pdbsum/3lsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsa ProSAT]</span></td></tr> | 
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lsa OCA], [http://pdbe.org/3lsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lsa RCSB], [http://www.ebi.ac.uk/pdbsum/3lsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lsa ProSAT]</span></td></tr> | + |  | 
|  | </table> |  | </table> | 
|  | == Evolutionary Conservation == |  | == Evolutionary Conservation == | 
| Line 34: | Line 33: | 
|  | [[Category: Large Structures]] |  | [[Category: Large Structures]] | 
|  | [[Category: Pectiniidae]] |  | [[Category: Pectiniidae]] | 
| - | [[Category: Brakemann, T]] | + | [[Category: Brakemann T]] | 
| - | [[Category: Jakobs, S]] | + | [[Category: Jakobs S]] | 
| - | [[Category: Trowitzsch, S]] | + | [[Category: Trowitzsch S]] | 
| - | [[Category: Wahl, M C]] | + | [[Category: Wahl MC]] | 
| - | [[Category: Weber, G]] | + | [[Category: Weber G]] | 
| - | [[Category: Beta barrel]]
 | + |  | 
| - | [[Category: Cis-trans isomerisation]]
 | + |  | 
| - | [[Category: Fluorescent protein]]
 | + |  | 
|  |   Structural highlights | 3lsa is a 4 chain structure with sequence from Pectiniidae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. 
 |  | Method: | X-ray diffraction, Resolution 1.79Å |  | Ligands: | , , , , |  | Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT | 
   Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
 
  Publication Abstract from PubMed Reversibly switchable fluorescent proteins can be repeatedly photoswitched between a fluorescent and a nonfluorescent state by irradiation with the light of two different wavelengths. The molecular basis of the switching process remains a controversial topic. Padron0.9 is a reversibly switchable fluorescent protein with "positive" switching characteristics, exhibiting excellent spectroscopic properties. Its chromophore is formed by the amino acids Cys-Tyr-Gly. We obtained high resolution x-ray structures of Padron0.9 in both the fluorescent and the nonfluorescent states and used the structural information for molecular dynamics simulations. We found that in Padron0.9 the chromophore undergoes a cis-trans isomerization upon photoswitching. The molecular dynamics simulations clarified the protonation states of the amino acid residues within the chromophore pocket that influence the protonation state of the chromophore. We conclude that a light driven cis-trans isomerization of the chromophore appears to be the fundamental switching mechanism in all photochromic fluorescent proteins known to date. Distinct absorption cross-sections for the switching wavelengths in the fluorescent and the nonfluorescent state are not essential for efficient photochromism in fluorescent proteins, although they may facilitate the switching process.
 Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron.,Brakemann T, Weber G, Andresen M, Groenhof G, Stiel AC, Trowitzsch S, Eggeling C, Grubmuller H, Hell SW, Wahl MC, Jakobs S J Biol Chem. 2010 May 7;285(19):14603-9. Epub 2010 Mar 16. PMID:20236929[1]
 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
   References ↑ Brakemann T, Weber G, Andresen M, Groenhof G, Stiel AC, Trowitzsch S, Eggeling C, Grubmuller H, Hell SW, Wahl MC, Jakobs S. Molecular basis of the light-driven switching of the photochromic fluorescent protein Padron. J Biol Chem. 2010 May 7;285(19):14603-9. Epub 2010 Mar 16. PMID:20236929 doi:10.1074/jbc.M109.086314
 
 |