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| - | [[Image:2v0u.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2v0u| PDB=2v0u | SCENE= }} | | {{STRUCTURE_2v0u| PDB=2v0u | SCENE= }} |
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| - | '''N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (CRYO DARK STRUCTURE OF LOV2 (404-546))'''
| + | ===N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (CRYO DARK STRUCTURE OF LOV2 (404-546))=== |
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| - | ==Overview==
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| - | Light sensing by photoreceptors controls phototropism, chloroplast movement, stomatal opening, and leaf expansion in plants. Understanding the molecular mechanism by which these processes are regulated requires a quantitative description of photoreceptor dynamics. We focus on a light-driven signal transduction mechanism in the LOV2 domain (LOV, light, oxygen, voltage) of the blue light photoreceptor phototropin 1 from Avena sativa (oat). High-resolution crystal structures of the dark and light states of an oat LOV2 construct including residues Leu404 through Leu546 (LOV2 (404-546)) have been determined at 105 and 293 K. In all four structures, LOV2 (404-546) exhibits the typical Per-ARNT-Sim (PAS) fold, flanked by an additional conserved N-terminal turn-helix-turn motif and a C-terminal flanking region containing an amphipathic Jalpha helix. These regions dock on the LOV2 core domain and bury several hydrophobic residues of the central beta-sheet of the core domain that would otherwise be exposed to solvent. Light structures of LOV2 (404-546) reveal that formation of the covalent bond between Cys450 and the C4a atom of the flavin mononucleotide (FMN) results in local rearrangement of the hydrogen-bonding network in the FMN binding pocket. These rearrangements are associated with disruption of the Asn414-Asp515 hydrogen bond on the surface of the protein and displacement of the N- and C-terminal flanking regions of LOV2 (404-546), both of which constitute a structural signal.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18001137}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18001137 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18001137}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Serine/threonine-protein kinase]] | | [[Category: Serine/threonine-protein kinase]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:59:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:22:02 2008'' |
Revision as of 01:22, 29 July 2008
Template:STRUCTURE 2v0u
N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (CRYO DARK STRUCTURE OF LOV2 (404-546))
Template:ABSTRACT PUBMED 18001137
About this Structure
2V0U is a Single protein structure of sequence from Avena sativa. Full crystallographic information is available from OCA.
Reference
N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa., Halavaty AS, Moffat K, Biochemistry. 2007 Dec 11;46(49):14001-9. Epub 2007 Nov 15. PMID:18001137
Page seeded by OCA on Tue Jul 29 04:22:02 2008
