|
|
| Line 1: |
Line 1: |
| | + | |
| | ==2.75 Angstrom resolution crystal structure of the A. thaliana LOV2 domain with an extended N-terminal A' helix (cryo dark structure)== | | ==2.75 Angstrom resolution crystal structure of the A. thaliana LOV2 domain with an extended N-terminal A' helix (cryo dark structure)== |
| | <StructureSection load='4hhd' size='340' side='right' caption='[[4hhd]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='4hhd' size='340' side='right' caption='[[4hhd]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HHD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. The March 2015 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HHD 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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOT1, JK224, NPH1, RPT1, At3g45780, T6D9_110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHOT1, JK224, NPH1, RPT1, At3g45780, T6D9_110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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='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='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=4hhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hhd RCSB], [http://www.ebi.ac.uk/pdbsum/4hhd PDBsum]</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=4hhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhd OCA], [http://pdbe.org/4hhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hhd RCSB], [http://www.ebi.ac.uk/pdbsum/4hhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| Line 18: |
Line 19: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4hhd" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Line 24: |
Line 26: |
| | [[Category: Arath]] | | [[Category: Arath]] |
| | [[Category: Non-specific serine/threonine protein kinase]] | | [[Category: Non-specific serine/threonine protein kinase]] |
| | + | [[Category: Phototropin]] |
| | + | [[Category: RCSB PDB Molecule of the Month]] |
| | [[Category: Halavaty, A S]] | | [[Category: Halavaty, A S]] |
| | [[Category: Moffat, K]] | | [[Category: Moffat, K]] |
| Structural highlights
4hhd is a 2 chain structure with sequence from Arath. The March 2015 RCSB PDB Molecule of the Month feature on Phototropin by David Goodsell is 10.2210/rcsb_pdb/mom_2015_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Gene: | PHOT1, JK224, NPH1, RPT1, At3g45780, T6D9_110 (ARATH) |
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PHOT1_ARATH] Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.[1] [2] [3] [4] [5] [6] [7] [8]
Publication Abstract from PubMed
A key role in signal transduction and dimerization mediated by Per-Arnt-Sim (PAS) domains is played by alpha-helical linkers that flank the structurally similar alpha/beta cores of these domains. However, crystal-packing forces and the different construct lengths and sequences of the PAS domains influence the final length and orientation of the linkers relative to the core and create uncertainty in the exact mechanism of the linker function. Thus, structural characterization and comparison of the linkers within isolated PAS-domain constructs and/or full-length PAS-containing proteins is important for clarification of the mechanism. The plant blue-light photoreceptors phototropins possess two N-terminal flavin mononucleotide-based light, oxygen or voltage (LOV) domains (LOV1 and LOV2) that comprise a subclass of the PAS family and one C-terminal serine/threonine kinase domain whose enzymatic activity is regulated by blue light. The dark-adapted state crystal structures of the Arabidopsis thaliana phototropin 1 and phototropin 2 LOV1-domain constructs flanked by an N-terminal A'alpha helix and the structure of the phototropin 2 core LOV2 domain are known. Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state. The core is flanked by an N-terminal A'alpha helix and a C-terminal Jalpha helix similar to those in the previously reported structure of Avena sativa phototropin 1 LOV2. In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer in which two A'alpha helices adopt a scissor-like orientation at the dimer interface and form a short alpha-helical coiled coil. The Jalpha helix predominantly interacts with the beta-sheet and plays a role in coiled-coil formation and dimerization.
Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana.,Halavaty AS, Moffat K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1316-21., doi: 10.1107/S1744309113029199. Epub 2013 Nov 28. PMID:24316821[9]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakai T, Wada T, Ishiguro S, Okada K. RPT2. A signal transducer of the phototropic response in Arabidopsis. Plant Cell. 2000 Feb;12(2):225-36. PMID:10662859
- ↑ Folta KM, Spalding EP. Unexpected roles for cryptochrome 2 and phototropin revealed by high-resolution analysis of blue light-mediated hypocotyl growth inhibition. Plant J. 2001 Jun;26(5):471-8. PMID:11439133
- ↑ Folta KM, Kaufman LS. Phototropin 1 is required for high-fluence blue-light-mediated mRNA destabilization. Plant Mol Biol. 2003 Mar;51(4):609-18. PMID:12650626
- ↑ 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
- ↑ Lariguet P, Schepens I, Hodgson D, Pedmale UV, Trevisan M, Kami C, de Carbonnel M, Alonso JM, Ecker JR, Liscum E, Fankhauser C. PHYTOCHROME KINASE SUBSTRATE 1 is a phototropin 1 binding protein required for phototropism. Proc Natl Acad Sci U S A. 2006 Jun 27;103(26):10134-9. Epub 2006 Jun 15. PMID:16777956 doi:http://dx.doi.org/10.1073/pnas.0603799103
- ↑ Sullivan S, Thomson CE, Lamont DJ, Jones MA, Christie JM. In vivo phosphorylation site mapping and functional characterization of Arabidopsis phototropin 1. Mol Plant. 2008 Jan;1(1):178-94. doi: 10.1093/mp/ssm017. Epub 2007 Dec 4. PMID:20031924 doi:http://dx.doi.org/10.1093/mp/ssm017
- ↑ Halavaty AS, Moffat K. Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1316-21., doi: 10.1107/S1744309113029199. Epub 2013 Nov 28. PMID:24316821 doi:http://dx.doi.org/10.1107/S1744309113029199
|
