View source for 4hhd


==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]] 2.75&Aring;' scene=''>
== Structural highlights ==
<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>
<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='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>
== Function ==
[[http://www.uniprot.org/uniprot/PHOT1_ARATH 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.<ref>PMID:10662859</ref> <ref>PMID:11439133</ref> <ref>PMID:12650626</ref> <ref>PMID:12821778</ref> <ref>PMID:15031408</ref> <ref>PMID:14982991</ref> <ref>PMID:16777956</ref> <ref>PMID:20031924</ref>  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24316821</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hhd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Phototropin]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Halavaty, A S]]
[[Category: Moffat, K]]
[[Category: Arabidopsis thaliana]]
[[Category: Atp-binding]]
[[Category: Kinase]]
[[Category: Light-induced signal transduction]]
[[Category: Lov2]]
[[Category: Phototropin-1]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]