1hcj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Photoproduct of the wild-type Aequorea victoria Green Fluorescent Protein== | ==Photoproduct of the wild-type Aequorea victoria Green Fluorescent Protein== | ||
<StructureSection load='1hcj' size='340' side='right' caption='[[1hcj]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1hcj' size='340' side='right' caption='[[1hcj]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hcj]] is a 4 chain structure | <table><tr><td colspan='2'>[[1hcj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HCJ FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b9c|1b9c]], [[1bfp|1bfp]], [[1c4f|1c4f]], [[1emb|1emb]], [[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emg|1emg]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[1f09|1f09]], [[1f0b|1f0b]], [[1yfp|1yfp]], [[2emd|2emd]], [[2emn|2emn]], [[2emo|2emo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b9c|1b9c]], [[1bfp|1bfp]], [[1c4f|1c4f]], [[1emb|1emb]], [[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emg|1emg]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[1f09|1f09]], [[1f0b|1f0b]], [[1yfp|1yfp]], [[2emd|2emd]], [[2emn|2emn]], [[2emo|2emo]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcj OCA], [http://pdbe.org/1hcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hcj RCSB], [http://www.ebi.ac.uk/pdbsum/1hcj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hcj ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hcj OCA], [http://pdbe.org/1hcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hcj RCSB], [http://www.ebi.ac.uk/pdbsum/1hcj PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 18: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hcj ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 36: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gensch, T]] | [[Category: Gensch, T]] | ||
[[Category: Hellingwerf, K J]] | [[Category: Hellingwerf, K J]] | ||
Revision as of 07:31, 21 September 2017
Photoproduct of the wild-type Aequorea victoria Green Fluorescent ProteinPhotoproduct of the wild-type Aequorea victoria Green Fluorescent Protein
Structural highlights
Function[GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. 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 PubMedWild type green fluorescent protein (GFP) from Aequorea victoria absorbs predominantly at 398 nm. Illumination with UV (254 nm) or visible (390 nm) light transforms this state (GFP(398)) into one absorbing at 483 nm (GFP(483)). Here we show that this photoconversion of GFP is a one-photon process that is paralleled by decarboxylation of Glu 222. We propose a mechanism in which decarboxylation is due to electron transfer between the gamma-carboxylate of Glu 222 and the p-hydroxybenzylidene-imidazolidinone chromophore of GFP, followed by reverse transfer of an electron and a proton to the remaining carbon side chain atom of Glu 222. Oxidative decarboxylation of a gamma-carboxylate represents a new type of posttranslational modification that may also occur in enzymes with high-potential reaction intermediates. Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222.,van Thor JJ, Gensch T, Hellingwerf KJ, Johnson LN Nat Struct Biol. 2002 Jan;9(1):37-41. PMID:11740505[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||