2z6d

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{{Seed}}
 
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[[Image:2z6d.png|left|200px]]
 
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==Crystal structure of LOV1 domain of phototropin2 from Arabidopsis thaliana==
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The line below this paragraph, containing "STRUCTURE_2z6d", creates the "Structure Box" on the page.
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<StructureSection load='2z6d' size='340' side='right'caption='[[2z6d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2z6d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. The March 2015 RCSB PDB [https://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 [https://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=2Z6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z6D FirstGlance]. <br>
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</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&#8491;</td></tr>
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<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>
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{{STRUCTURE_2z6d| PDB=2z6d | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2z6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6d OCA], [https://pdbe.org/2z6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z6d RCSB], [https://www.ebi.ac.uk/pdbsum/2z6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z6d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z6/2z6d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z6d ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phototropin (phot) is a blue-light receptor protein that triggers phototropic responses, chloroplast relocation, and stomata opening to maximize the efficiency of photosynthesis in higher plants. Phot is composed of three functional domains. The N-terminal half folds into two light-oxygen-voltage-sensing domains called LOV1 and LOV2, each binding a flavin mononucleotide to absorb blue light. The C-terminal half is a serine/threonine kinase domain that causes light-dependent autophosphorylation leading to cellular signaling cascades. LOV2 domain is primarily responsible for activation of the kinase, and LOV1 domain is thought to act as a dimerization site and to regulate sensitivity to activation by blue light. Here we show the crystal structures of LOV1 domains of Arabidopsis phot1 and phot2 in the dark at resolutions of 2.1 A and 2.0 A, respectively. Either LOV1 domain forms a dimer through face-to-face association of beta-scaffolds in the crystallographic asymmetric unit. Three types of interactions stabilizing the dimer structures found are as follows: contacts of side chains in their beta-scaffolds, hydrophobic interactions of a short helix found in the N-terminus of a subunit with the beta-scaffolds of both subunits, and hydrogen bonds mediated by hydration water molecules filling the dimer interface. The critical residues for dimerization are Cys261, forming a disulfide bridge between subunits in phot1-LOV1 domain, and Thr217 and Met232 in phot2-LOV1. The topology in homodimeric associations of the LOV1 domains is discussed when referring to those of homodimers or heterodimers of light-oxygen-voltage-sensing or Per-ARNT-Sim domains. The present results also provide clues to understanding structural basis in dimeric interactions of Per-ARNT-Sim protein modules in cellular signaling.
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===Crystal structure of LOV1 domain of phototropin2 from Arabidopsis thaliana===
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Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2.,Nakasako M, Zikihara K, Matsuoka D, Katsura H, Tokutomi S J Mol Biol. 2008 Sep 5;381(3):718-33. Epub 2008 Jun 18. PMID:18585389<ref>PMID:18585389</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_18585389}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2z6d" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18585389 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18585389}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2Z6D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z6D OCA].
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==Reference==
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Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2., Nakasako M, Zikihara K, Matsuoka D, Katsura H, Tokutomi S, J Mol Biol. 2008 Sep 5;381(3):718-33. Epub 2008 Jun 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18585389 18585389]
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Crystallization and preliminary X-ray diffraction analysis of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thaliana., Nakasako M, Hirata M, Shimizu N, Hosokawa S, Matsuoka D, Oka T, Yamamoto M, Tokutomi S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt, 7):617-21. Epub 2008 Jun 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18607090 18607090]
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Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering., Nakasako M, Iwata T, Matsuoka D, Tokutomi S, Biochemistry. 2004 Nov 30;43(47):14881-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15554695 15554695]
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Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 protein., Nakasako M, Matsuoka D, Zikihara K, Tokutomi S, FEBS Lett. 2005 Feb 14;579(5):1067-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15710392 15710392]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Phototropin]]
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[[Category: Matsuoka, D.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Nakasako, M.]]
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[[Category: Matsuoka D]]
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[[Category: Tokutomi, S.]]
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[[Category: Nakasako M]]
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[[Category: Alternative splicing]]
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[[Category: Tokutomi S]]
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[[Category: Atp-binding]]
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[[Category: Chromophore]]
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[[Category: Flavoprotein]]
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[[Category: Fmn]]
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[[Category: Kinase]]
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[[Category: Lov-fold]]
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[[Category: Membrane]]
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[[Category: Nucleotide-binding]]
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[[Category: Pas-fold]]
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[[Category: Phosphorylation]]
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[[Category: Photoreceptor protein]]
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[[Category: Receptor]]
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[[Category: Sensory transduction]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 1 21:17:52 2008''
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Current revision

Crystal structure of LOV1 domain of phototropin2 from Arabidopsis thaliana

PDB ID 2z6d

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