2okw: Difference between revisions

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[[Image:2okw.png|left|200px]]


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==A non-invasive GFP-based biosensor for mercury ions==
The line below this paragraph, containing "STRUCTURE_2okw", creates the "Structure Box" on the page.
<StructureSection load='2okw' size='340' side='right'caption='[[2okw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2okw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OKW FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr>
{{STRUCTURE_2okw|  PDB=2okw  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2okw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2okw OCA], [https://pdbe.org/2okw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2okw RCSB], [https://www.ebi.ac.uk/pdbsum/2okw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2okw ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/2okw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2okw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mercury is a ubiquitous pollutant that when absorbed is extremely toxic to a wide variety of biochemical processes. Mercury (II) is a strong, "invisible" poison that is rapidly absorbed by tissues of the intestinal tract, kidneys, and liver upon ingestion. In this study, a novel fluorescence-based biosensor is presented that allows for the direct monitoring of the uptake and distribution of the metal under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, located in close proximity to the chromophore, the green fluorescent protein (GFP) from Aequorea victoria was converted into a highly specific biosensor for this metal ion. The mutant protein exhibits a dramatic absorbance and fluorescence change upon mercuration at neutral pH. Absorbance and fluorescence properties with respect to the metal concentration exhibit sigmoidal binding behavior with a detection limit in the low nanomolar range. Time-resolved binding studies indicate rapid subsecond binding of the metal to the protein. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein. To our knowledge, this engineered protein is a first example of a biosensor that allows for noninvasive and real-time imaging of mercury uptake in a living cell. A major advantage is that its expression can be genetically controlled in many organisms to enable unprecedented studies of tissue specific mercury uptake.


===A non-invasive GFP-based biosensor for mercury ions===
Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake.,Chapleau RR, Blomberg R, Ford PC, Sagermann M Protein Sci. 2008 Apr;17(4):614-22. Epub 2008 Feb 27. PMID:18305194<ref>PMID:18305194</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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{{ABSTRACT_PUBMED_18305194}}
 
==About this Structure==
[[2okw]] is a 6 chain structure of [[Green Fluorescent Protein]] with sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKW OCA].


==See Also==
==See Also==
*[[Green Fluorescent Protein]]
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:18305194</ref><ref group="xtra">PMID:14684834</ref><ref group="xtra">PMID:8703075</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Aequorea victoria]]
[[Category: Aequorea victoria]]
[[Category: Blomberg, R.]]
[[Category: Large Structures]]
[[Category: Chapleau, R R.]]
[[Category: Blomberg R]]
[[Category: Ford, P C.]]
[[Category: Chapleau RR]]
[[Category: Sagermann, M.]]
[[Category: Ford PC]]
[[Category: Biosensor]]
[[Category: Sagermann M]]
[[Category: Luminescent protein]]
[[Category: Mercury]]

Latest revision as of 08:24, 17 October 2024

A non-invasive GFP-based biosensor for mercury ionsA non-invasive GFP-based biosensor for mercury ions

Structural highlights

2okw is a 6 chain structure with sequence from Aequorea victoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
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

Mercury is a ubiquitous pollutant that when absorbed is extremely toxic to a wide variety of biochemical processes. Mercury (II) is a strong, "invisible" poison that is rapidly absorbed by tissues of the intestinal tract, kidneys, and liver upon ingestion. In this study, a novel fluorescence-based biosensor is presented that allows for the direct monitoring of the uptake and distribution of the metal under noninvasive in vivo conditions. With the introduction of a cysteine residue at position 205, located in close proximity to the chromophore, the green fluorescent protein (GFP) from Aequorea victoria was converted into a highly specific biosensor for this metal ion. The mutant protein exhibits a dramatic absorbance and fluorescence change upon mercuration at neutral pH. Absorbance and fluorescence properties with respect to the metal concentration exhibit sigmoidal binding behavior with a detection limit in the low nanomolar range. Time-resolved binding studies indicate rapid subsecond binding of the metal to the protein. The crystal structures obtained of mutant eGFP205C indicate a possible access route of the metal into the core of the protein. To our knowledge, this engineered protein is a first example of a biosensor that allows for noninvasive and real-time imaging of mercury uptake in a living cell. A major advantage is that its expression can be genetically controlled in many organisms to enable unprecedented studies of tissue specific mercury uptake.

Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake.,Chapleau RR, Blomberg R, Ford PC, Sagermann M Protein Sci. 2008 Apr;17(4):614-22. Epub 2008 Feb 27. PMID:18305194[1]

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

See Also

References

  1. Chapleau RR, Blomberg R, Ford PC, Sagermann M. Design of a highly specific and noninvasive biosensor suitable for real-time in vivo imaging of mercury (II) uptake. Protein Sci. 2008 Apr;17(4):614-22. Epub 2008 Feb 27. PMID:18305194 doi:10.1110/ps.073358908

2okw, resolution 1.90Å

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