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| | <StructureSection load='6qqj' size='340' side='right'caption='[[6qqj]], [[Resolution|resolution]] 2.08Å' scene=''> | | <StructureSection load='6qqj' size='340' side='right'caption='[[6qqj]], [[Resolution|resolution]] 2.08Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qqj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QQJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qqj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QQJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 2.08Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=6qqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqj OCA], [http://pdbe.org/6qqj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qqj RCSB], [http://www.ebi.ac.uk/pdbsum/6qqj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqj 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=6qqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qqj OCA], [https://pdbe.org/6qqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qqj RCSB], [https://www.ebi.ac.uk/pdbsum/6qqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qqj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHOT2_ARATH PHOT2_ARATH]] Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.<ref>PMID:11371609</ref> <ref>PMID:11251116</ref> <ref>PMID:12821778</ref> <ref>PMID:15031408</ref> <ref>PMID:14982991</ref> | + | [https://www.uniprot.org/uniprot/PHOT2_ARATH PHOT2_ARATH] Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.<ref>PMID:11371609</ref> <ref>PMID:11251116</ref> <ref>PMID:12821778</ref> <ref>PMID:15031408</ref> <ref>PMID:14982991</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources. |
| | + | |
| | + | Specific radiation damage is a lesser concern at room temperature.,Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810<ref>PMID:31316810</ref> |
| | + | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 6qqj" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Aumonier S]] |
| - | [[Category: Aumonier, S]] | + | [[Category: Gotthard G]] |
| - | [[Category: Gotthard, G]] | + | [[Category: Royant A]] |
| - | [[Category: Royant, A]] | + | |
| - | [[Category: Cryo-crystallography]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Room temperature macromolecular crystallography]]
| + | |
| - | [[Category: Specific radiation damage]]
| + | |
| - | [[Category: Time-resolved crystallography]]
| + | |
| Structural highlights
Function
PHOT2_ARATH Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.
Specific radiation damage is a lesser concern at room temperature.,Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakai T, Kagawa T, Kasahara M, Swartz TE, Christie JM, Briggs WR, Wada M, Okada K. Arabidopsis nph1 and npl1: blue light receptors that mediate both phototropism and chloroplast relocation. Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6969-74. Epub 2001 May 22. PMID:11371609 doi:http://dx.doi.org/10.1073/pnas.101137598
- ↑ Kagawa T, Sakai T, Suetsugu N, Oikawa K, Ishiguro S, Kato T, Tabata S, Okada K, Wada M. Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-light avoidance response. Science. 2001 Mar 16;291(5511):2138-41. PMID:11251116 doi:http://dx.doi.org/10.1126/science.291.5511.2138
- ↑ Harada A, Sakai T, Okada K. Phot1 and phot2 mediate blue light-induced transient increases in cytosolic Ca2+ differently in Arabidopsis leaves. Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8583-8. Epub 2003 Jun 23. PMID:12821778 doi:http://dx.doi.org/10.1073/pnas.1336802100
- ↑ Inada S, Ohgishi M, Mayama T, Okada K, Sakai T. RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana. Plant Cell. 2004 Apr;16(4):887-96. Epub 2004 Mar 18. PMID:15031408 doi:http://dx.doi.org/10.1105/tpc.019901
- ↑ Ohgishi M, Saji K, Okada K, Sakai T. Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis. Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2223-8. PMID:14982991
- ↑ Gotthard G, Aumonier S, De Sanctis D, Leonard G, von Stetten D, Royant A. Specific radiation damage is a lesser concern at room temperature. IUCrJ. 2019 Jun 12;6(Pt 4):665-680. doi: 10.1107/S205225251900616X. eCollection, 2019 Jul 1. PMID:31316810 doi:http://dx.doi.org/10.1107/S205225251900616X
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