4y5f: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4y5f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y5F FirstGlance]. <br>
<table><tr><td colspan='2'>[[4y5f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y5F FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LBV:3-[2-[(Z)-[3-(2-CARBOXYETHYL)-5-[(Z)-(4-ETHENYL-3-METHYL-5-OXIDANYLIDENE-PYRROL-2-YLIDENE)METHYL]-4-METHYL-PYRROL-1-IUM-2-YLIDENE]METHYL]-5-[(Z)-[(3E)-3-ETHYLIDENE-4-METHYL-5-OXIDANYLIDENE-PYRROLIDIN-2-YLIDENE]METHYL]-4-METHYL-1H-PYRROL-3-YL]PROPANOIC+ACID'>LBV</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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LBV:3-[2-[(Z)-[3-(2-CARBOXYETHYL)-5-[(Z)-(4-ETHENYL-3-METHYL-5-OXIDANYLIDENE-PYRROL-2-YLIDENE)METHYL]-4-METHYL-PYRROL-1-IUM-2-YLIDENE]METHYL]-5-[(Z)-[(3E)-3-ETHYLIDENE-4-METHYL-5-OXIDANYLIDENE-PYRROLIDIN-2-YLIDENE]METHYL]-4-METHYL-1H-PYRROL-3-YL]PROPANOIC+ACID'>LBV</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=4y5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y5f OCA], [https://pdbe.org/4y5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y5f RCSB], [https://www.ebi.ac.uk/pdbsum/4y5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y5f 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=4y5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y5f OCA], [https://pdbe.org/4y5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y5f RCSB], [https://www.ebi.ac.uk/pdbsum/4y5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y5f ProSAT]</span></td></tr>
</table>
</table>

Latest revision as of 10:54, 27 September 2023

PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, high dosePAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, high dose

Structural highlights

4y5f is a 1 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BPHY_DEIRA Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region. Has also a slight blue shift for the far-red maximum. Could also absorb green light. May participate in regulating pigment synthesis like the carotenoid deinoxanthin which could protect the bacterium from intense visible light.

Publication Abstract from PubMed

We report that in the red light-absorbing (Pr) state, the bilin chromophore of the Deinococcus radiodurans proteobacterial phytochrome (DrBphP) is hypersensitive to X-ray photons used in typical synchrotron X-ray protein crystallography experiments. This causes the otherwise fully protonated chromophore to deprotonate without additional major structural changes. These results have major implications for our understanding of the structural and chemical characteristics of the resting and intermediate states of phytochromes and other photoreceptor proteins.

X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome.,Li F, Burgie ES, Yu T, Heroux A, Schatz GC, Vierstra RD, Orville AM J Am Chem Soc. 2015 Mar 4;137(8):2792-5. doi: 10.1021/ja510923m. Epub 2015 Feb, 18. PMID:25650486[1]

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

References

  1. Li F, Burgie ES, Yu T, Heroux A, Schatz GC, Vierstra RD, Orville AM. X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome. J Am Chem Soc. 2015 Mar 4;137(8):2792-5. doi: 10.1021/ja510923m. Epub 2015 Feb, 18. PMID:25650486 doi:http://dx.doi.org/10.1021/ja510923m

4y5f, resolution 1.70Å

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OCA