2pr5

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(Difference between revisions)

Revision as of 09:31, 18 October 2017

Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)

Structural highlights

2pr5 is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. The March 2015 RCSB PDB Molecule of the Month feature on Phototropin by David Goodsell is 10.2210/rcsb_pdb/mom_2015_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	2pr6
Gene:	pfyP ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PHOT_BACSU] Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The photosensor YtvA binds flavin mononucleotide and regulates the general stress reaction in Bacillus subtilis in response to blue light illumination. It belongs to the family of light-oxygen-voltage (LOV) proteins that were first described in plant phototropins and form a subgroup of the Per-Arnt-Sim (PAS) superfamily. Here, we report the three-dimensional structure of the LOV domain of YtvA in its dark and light states. The protein assumes the global fold common to all PAS domains and dimerizes via a hydrophobic interface. Directly C-terminal to the core of the LOV domain, an alpha-helix extends into the solvent. Light absorption causes formation of a covalent bond between a conserved cysteine residue and atom C(4a) of the FMN ring, which triggers rearrangements throughout the LOV domain. Concomitantly, in the dark and light structures, the two subunits of the dimeric protein rotate relative to each other by 5 degrees . This small quaternary structural change is presumably a component of the mechanism by which the activity of YtvA is regulated in response to light. In terms of both structure and signaling mechanism, YtvA differs from plant phototropins and more closely resembles prokaryotic heme-binding PAS domains.

Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.,Moglich A, Moffat K J Mol Biol. 2007 Oct 12;373(1):112-26. Epub 2007 Aug 2. PMID:17764689^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, Price CW. New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J Bacteriol. 2001 Feb;183(4):1329-38. PMID:11157946 doi:10.1128/JB.183.4.1329-1338.2001
↑ Moglich A, Moffat K. Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA. J Mol Biol. 2007 Oct 12;373(1):112-26. Epub 2007 Aug 2. PMID:17764689 doi:10.1016/j.jmb.2007.07.039

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pr5"

@@ Line 1: / Line 1: @@
 ==Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)==
 <StructureSection load='2pr5' size='340' side='right' caption='[[2pr5]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pr6|2pr6]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pfyP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=2pr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pr5 OCA], [http://pdbe.org/2pr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pr5 RCSB], [http://www.ebi.ac.uk/pdbsum/2pr5 PDBsum]</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=2pr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pr5 OCA], [http://pdbe.org/2pr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pr5 RCSB], [http://www.ebi.ac.uk/pdbsum/2pr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pr5 ProSAT]</span></td></tr>
 </table>
 == Function ==

2pr5

From Proteopedia

Revision as of 09:31, 18 October 2017

Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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