1g28: Difference between revisions

Revision as of 04:17, 1 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:1g28.png

1g28, resolution 2.73Å ()

Ligands:

Gene:

PHY3 (Adiantum capillus-veneris)

Structural annotation:
Resources:	CATH : 1G28A00, 1G28B00, 1G28C00, 1G28D00 InterPro : Ipr003018, Ipr001294, Ipr002290, Ipr000719, Ipr013515, Ipr013654, Ipr013516, Ipr000700, Ipr013655, Ipr011009, Ipr001610, Ipr008271, Ipr000014 Pfam : PF08447 SCOP : d1g28a_, d1g28b_, d1g28c_, d1g28d_ UniProt : Q9ZWQ6

Functional annotation:
Biological process:	sensory perception regulation of transcription protein-chromophore linkage protein amino acid phosphorylation two-component signal transduction system (phosphorelay) signal transduction regulation of transcription, DNA-dependent
Molecular function:	nucleotide binding receptor activity signal transducer activity G-protein coupled photoreceptor activity ATP binding protein serine/threonine kinase activity two-component sensor activity transferase activity protein kinase activity photoreceptor activity kinase activity

Evolutionary conservation:

Toggle Conservation Colors:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

STRUCTURE OF A FLAVIN-BINDING DOMAIN, LOV2, FROM THE CHIMERIC PHYTOCHROME/PHOTOTROPIN PHOTORECEPTOR PHY3STRUCTURE OF A FLAVIN-BINDING DOMAIN, LOV2, FROM THE CHIMERIC PHYTOCHROME/PHOTOTROPIN PHOTORECEPTOR PHY3

Template:ABSTRACT PUBMED 11248020

About this StructureAbout this Structure

1G28 is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction., Crosson S, Moffat K, Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):2995-3000. Epub 2001 Feb 27. PMID:11248020

Page seeded by OCA on Tue Jul 1 04:17:57 2008

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OCA

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-'''STRUCTURE OF A FLAVIN-BINDING DOMAIN, LOV2, FROM THE CHIMERIC PHYTOCHROME/PHOTOTROPIN PHOTORECEPTOR PHY3'''
+===STRUCTURE OF A FLAVIN-BINDING DOMAIN, LOV2, FROM THE CHIMERIC PHYTOCHROME/PHOTOTROPIN PHOTORECEPTOR PHY3===
-==Overview==
+<!--
-Phototropin, a major blue-light receptor for phototropism in seed plants, exhibits blue-light-dependent autophosphorylation and contains two light, oxygen, or voltage (LOV) domains and a serine/threonine kinase domain. The LOV domains share homology with the PER-ARNT-SIM (PAS) superfamily, a diverse group of sensor proteins. Each LOV domain noncovalently binds a single FMN molecule and exhibits reversible photochemistry in vitro when expressed separately or in tandem. We have determined the crystal structure of the LOV2 domain from the phototropin segment of the chimeric fern photoreceptor phy3 to 2.7-A resolution. The structure constitutes an FMN-binding fold that reveals how the flavin cofactor is embedded in the protein. The single LOV2 cysteine residue is located 4.2 A from flavin atom C(4a), consistent with a model in which absorption of blue light induces formation of a covalent cysteinyl-C(4a) adduct. Residues that interact with FMN in the phototropin segment of the chimeric fern photoreceptor (phy3) LOV2 are conserved in LOV domains from phototropin of other plant species and from three proteins involved in the regulation of circadian rhythms in Arabidopsis and Neurospora. This conservation suggests that these domains exhibit the same overall fold and share a common mechanism for flavin binding and light-induced signaling.
+The line below this paragraph, {{ABSTRACT_PUBMED_11248020}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11248020 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11248020}}
 ==About this Structure==
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 [[Category: Photoreceptor]]
 [[Category: Phototropin]]
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