1hcj: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hcj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. 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> | <table><tr><td colspan='2'>[[1hcj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. 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><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><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr> | ||
<tr><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://www.rcsb.org/pdb/explore.do?structureId=1hcj RCSB], [http://www.ebi.ac.uk/pdbsum/1hcj PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=1hcj RCSB], [http://www.ebi.ac.uk/pdbsum/1hcj PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aeqvi]] | [[Category: Aeqvi]] | ||
[[Category: Gensch, T | [[Category: Gensch, T]] | ||
[[Category: Hellingwerf, K J | [[Category: Hellingwerf, K J]] | ||
[[Category: Johnson, L | [[Category: Johnson, L]] | ||
[[Category: Thor, J J.Van | [[Category: Thor, J J.Van]] | ||
[[Category: Beta-barrel]] | [[Category: Beta-barrel]] | ||
[[Category: Bioluminescence]] | [[Category: Bioluminescence]] | ||
Revision as of 03:30, 23 December 2014
Photoproduct of the wild-type Aequorea victoria Green Fluorescent ProteinPhotoproduct of the wild-type Aequorea victoria Green Fluorescent Protein
Structural highlights
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
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