2a56: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='2a56' size='340' side='right'caption='[[2a56]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2a56' size='340' side='right'caption='[[2a56]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2a56]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anesu Anesu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A56 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2a56]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anemonia_sulcata Anemonia sulcata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A56 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2a50|2a50]], [[2a52|2a52]], [[2a53|2a53]], [[2a54|2a54]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NRQ:{(4Z)-4-(4-HYDROXYBENZYLIDENE)-2-[3-(METHYLTHIO)PROPANIMIDOYL]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>NRQ</scene></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=2a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a56 OCA], [https://pdbe.org/2a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a56 RCSB], [https://www.ebi.ac.uk/pdbsum/2a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a56 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=2a56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a56 OCA], [https://pdbe.org/2a56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a56 RCSB], [https://www.ebi.ac.uk/pdbsum/2a56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a56 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NFCP_ANESU NFCP_ANESU]] Pigment protein that is intensely purple in color.<ref>PMID:10852900</ref>
[https://www.uniprot.org/uniprot/NFCP_ANESU NFCP_ANESU] Pigment protein that is intensely purple in color.<ref>PMID:10852900</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 33: Line 33:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anesu]]
[[Category: Anemonia sulcata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Andresen, M]]
[[Category: Andresen M]]
[[Category: Eggeling, C]]
[[Category: Eggeling C]]
[[Category: Graeter, F]]
[[Category: Graeter F]]
[[Category: Grubmueller, H]]
[[Category: Grubmueller H]]
[[Category: Hell, S W]]
[[Category: Hell SW]]
[[Category: Jakobs, S]]
[[Category: Jakobs S]]
[[Category: Schaefer, L]]
[[Category: Schaefer L]]
[[Category: Stiel, A C]]
[[Category: Stiel AC]]
[[Category: Trowitzsch, S]]
[[Category: Trowitzsch S]]
[[Category: Wahl, M C]]
[[Category: Wahl MC]]
[[Category: Weber, G]]
[[Category: Weber G]]
[[Category: Ascp]]
[[Category: Chromoprotein]]
[[Category: Fluorescent protein]]
[[Category: Luminescent protein]]
[[Category: Photochromic protein]]
[[Category: Reversible photoswitch]]

Latest revision as of 11:15, 15 May 2024

fluorescent protein asFP595, A143S, on-state, 5min irradiationfluorescent protein asFP595, A143S, on-state, 5min irradiation

Structural highlights

2a56 is a 4 chain structure with sequence from Anemonia sulcata. 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

NFCP_ANESU Pigment protein that is intensely purple in color.[1]

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

Proteins that can be reversibly photoswitched between a fluorescent and a nonfluorescent state bear enormous potential in diverse fields, such as data storage, in vivo protein tracking, and subdiffraction resolution light microscopy. However, these proteins could hitherto not live up to their full potential because the molecular switching mechanism is not resolved. Here, we clarify the molecular photoswitching mechanism of asFP595, a green fluorescent protein (GFP)-like protein that can be transferred from a nonfluorescent "off" to a fluorescent "on" state and back again, by green and blue light, respectively. To this end, we establish reversible photoswitching of fluorescence in whole protein crystals and show that the switching kinetics in the crystal is identical with that in solution. Subsequent x-ray analysis demonstrated that upon the absorption of a green photon, the chromophore isomerizes from a trans (off) to a cis (on) state. Molecular dynamics calculations suggest that isomerization occurs through a bottom hula twist mechanism with concomitant rotation of both bonds of the chromophoric methine ring bridge. This insight into the switching mechanism should facilitate the targeted design of photoswitchable proteins. Reversible photoswitching of the protein chromophore system within intact crystals also constitutes a step toward the use of fluorescent proteins in three-dimensional data recording.

Structure and mechanism of the reversible photoswitch of a fluorescent protein.,Andresen M, Wahl MC, Stiel AC, Grater F, Schafer LV, Trowitzsch S, Weber G, Eggeling C, Grubmuller H, Hell SW, Jakobs S Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13070-4. Epub 2005 Aug 31. PMID:16135569[2]

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

References

  1. Lukyanov KA, Fradkov AF, Gurskaya NG, Matz MV, Labas YA, Savitsky AP, Markelov ML, Zaraisky AG, Zhao X, Fang Y, Tan W, Lukyanov SA. Natural animal coloration can Be determined by a nonfluorescent green fluorescent protein homolog. J Biol Chem. 2000 Aug 25;275(34):25879-82. PMID:10852900 doi:http://dx.doi.org/10.1074/jbc.C000338200
  2. Andresen M, Wahl MC, Stiel AC, Grater F, Schafer LV, Trowitzsch S, Weber G, Eggeling C, Grubmuller H, Hell SW, Jakobs S. Structure and mechanism of the reversible photoswitch of a fluorescent protein. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13070-4. Epub 2005 Aug 31. PMID:16135569

2a56, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA