4y5f: Difference between revisions
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''' | ==PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, high dose== | ||
<StructureSection load='4y5f' size='340' side='right' caption='[[4y5f]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4y5f]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y5F FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y3i|4y3i]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </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=4y5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y5f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y5f RCSB], [http://www.ebi.ac.uk/pdbsum/4y5f PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/BPHY_DEIRA 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. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:25650486</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Histidine kinase]] | |||
[[Category: Burgie, E S]] | |||
[[Category: Heroux, A]] | |||
[[Category: Li, F]] | |||
[[Category: Orville, A M]] | |||
[[Category: Schatz, G C]] | |||
[[Category: Vierstra, R D]] | |||
[[Category: Yu, T]] | [[Category: Yu, T]] | ||
[[Category: | [[Category: Bilin chromophore]] | ||
[[Category: | [[Category: High-dose]] | ||
[[Category: | [[Category: Phythochrome]] | ||
[[Category: | [[Category: Spectroscopy]] | ||
[[Category: | [[Category: Transferase]] | ||
Revision as of 15:08, 20 May 2015
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
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 PubMedWe 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
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