2v1a: Difference between revisions

Revision as of 05:37, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2v1a.png

Template:STRUCTURE 2v1a

N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (ROOM TEMPERATURE (293K) DARK STRUCTURE OF LOV2 (404-546))N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (ROOM TEMPERATURE (293K) DARK STRUCTURE OF LOV2 (404-546))

Template:ABSTRACT PUBMED 18001137

About this StructureAbout this Structure

2V1A is a Single protein structure of sequence from Avena sativa. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2v1a|  PDB=2v1a  |  SCENE=  }}
-'''N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (ROOM TEMPERATURE (293K) DARK STRUCTURE OF LOV2 (404-546))'''
+===N- AND C-TERMINAL HELICES OF OAT LOV2 (404-546) ARE INVOLVED IN LIGHT-INDUCED SIGNAL TRANSDUCTION (ROOM TEMPERATURE (293K) DARK STRUCTURE OF LOV2 (404-546))===
-==Overview==
+<!--
-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
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
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