1w7u

From Proteopedia

(Difference between revisions)

Revision as of 06:29, 6 October 2021

Photoproduct of the Wild-Type Aequorea victoria Green Fluorescent Protein after structural annealing at 170K

Structural highlights

1w7u is a 4 chain structure with sequence from Aeqvi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Related:	1b9c, 1bfp, 1c4f, 1cv7, 1ema, 1emb, 1emc, 1eme, 1emf, 1emg, 1emk, 1eml, 1emm, 1f09, 1f0b, 1gfl, 1h6r, 1hcj, 1huy, 1jby, 1jbz, 1jc0, 1jc1, 1kp5, 1kyp, 1kyr, 1kys, 1myw, 1q4a, 1q4b, 1q4c, 1q4d, 1q4e, 1q73, 1qxt, 1qy3, 1qyf, 1qyo, 1qyq, 1rm9, 1rmm, 1rmo, 1rmp, 1rrx, 1w7s, 1yfp, 2emd, 2emn, 2emo
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Green fluorescent protein (GFP) fluoresces efficiently under blue excitation despite major electrostatic rearrangements resulting from photoionization of the chromophore and neutralization of Glu-222. A competing phototransformation process, which ionizes the chromophore and decarboxylates Glu-222, mimics the electrostatic and structural changes in the fluorescence photocycle. Structural and spectroscopic analysis of the cryogenically stabilized photoproduct at 100 K and a structurally annealed intermediate of the phototransformed protein at 170 K reveals distinct structural relaxations involving protein, chromophore, solvent, and photogenerated CO2. Strong structural changes of the 100 K photoproduct after decarboxylation appear exclusively within 15 angstroms of the chromophore and include the electrostatically driven perturbations of Gln-69, Cys-70, and water molecules in an H-bonding network connecting the chromophore. X-ray crystallography to 1.85 angstroms resolution and static and picosecond time-resolved IR spectroscopy identify structural mechanisms common to phototransformation and to the fluorescence photocycle. In particular, the appearance of a 1697 cm(-1) (+) difference band in both photocycle and phototransformation intermediates is a spectroscopic signature for the structural perturbation of Gln-69. This is taken as evidence for an electrostatically driven dynamic response that is common to both photoreaction pathways. The interactions between the chromophore and the perturbed residues and solvent are decreased or removed in the T203H single and T203H/Q69L double mutants, resulting in a strong reduction of the fluorescence quantum yield. This suggests that the electrostatic response to the transient formation of a buried charge in the wild type is important for the bright fluorescence.

Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein.,van Thor JJ, Georgiev GY, Towrie M, Sage JT J Biol Chem. 2005 Sep 30;280(39):33652-9. Epub 2005 Jul 20. PMID:16033764^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ van Thor JJ, Georgiev GY, Towrie M, Sage JT. Ultrafast and low barrier motions in the photoreactions of the green fluorescent protein. J Biol Chem. 2005 Sep 30;280(39):33652-9. Epub 2005 Jul 20. PMID:16033764 doi:10.1074/jbc.M505473200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w7u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1w7u' size='340' side='right'caption='[[1w7u]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w7u]] 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=1W7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w7u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7U 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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b9c|1b9c]], [[1bfp|1bfp]], [[1c4f|1c4f]], [[1cv7|1cv7]], [[1ema|1ema]], [[1emb|1emb]], [[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emg|1emg]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[1f09|1f09]], [[1f0b|1f0b]], [[1gfl|1gfl]], [[1h6r|1h6r]], [[1hcj|1hcj]], [[1huy|1huy]], [[1jby|1jby]], [[1jbz|1jbz]], [[1jc0|1jc0]], [[1jc1|1jc1]], [[1kp5|1kp5]], [[1kyp|1kyp]], [[1kyr|1kyr]], [[1kys|1kys]], [[1myw|1myw]], [[1q4a|1q4a]], [[1q4b|1q4b]], [[1q4c|1q4c]], [[1q4d|1q4d]], [[1q4e|1q4e]], [[1q73|1q73]], [[1qxt|1qxt]], [[1qy3|1qy3]], [[1qyf|1qyf]], [[1qyo|1qyo]], [[1qyq|1qyq]], [[1rm9|1rm9]], [[1rmm|1rmm]], [[1rmo|1rmo]], [[1rmp|1rmp]], [[1rrx|1rrx]], [[1w7s|1w7s]], [[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"><div style='overflow: auto; max-height: 3em;'>[[1b9c|1b9c]], [[1bfp|1bfp]], [[1c4f|1c4f]], [[1cv7|1cv7]], [[1ema|1ema]], [[1emb|1emb]], [[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emg|1emg]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[1f09|1f09]], [[1f0b|1f0b]], [[1gfl|1gfl]], [[1h6r|1h6r]], [[1hcj|1hcj]], [[1huy|1huy]], [[1jby|1jby]], [[1jbz|1jbz]], [[1jc0|1jc0]], [[1jc1|1jc1]], [[1kp5|1kp5]], [[1kyp|1kyp]], [[1kyr|1kyr]], [[1kys|1kys]], [[1myw|1myw]], [[1q4a|1q4a]], [[1q4b|1q4b]], [[1q4c|1q4c]], [[1q4d|1q4d]], [[1q4e|1q4e]], [[1q73|1q73]], [[1qxt|1qxt]], [[1qy3|1qy3]], [[1qyf|1qyf]], [[1qyo|1qyo]], [[1qyq|1qyq]], [[1rm9|1rm9]], [[1rmm|1rmm]], [[1rmo|1rmo]], [[1rmp|1rmp]], [[1rrx|1rrx]], [[1w7s|1w7s]], [[1yfp|1yfp]], [[2emd|2emd]], [[2emn|2emn]], [[2emo|2emo]]</div></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=1w7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7u OCA], [http://pdbe.org/1w7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w7u RCSB], [http://www.ebi.ac.uk/pdbsum/1w7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7u 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=1w7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7u OCA], [https://pdbe.org/1w7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7u RCSB], [https://www.ebi.ac.uk/pdbsum/1w7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GFP_AEQVI 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.
+[[https://www.uniprot.org/uniprot/GFP_AEQVI 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1w7u

From Proteopedia

Revision as of 06:29, 6 October 2021

Photoproduct of the Wild-Type Aequorea victoria Green Fluorescent Protein after structural annealing at 170K

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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