2pd7: Difference between revisions

Revision as of 19:28, 21 February 2008

2.0 Angstrom Crystal Structure of the Fungal Blue-Light Photoreceptor Vivid

OverviewOverview

The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).

About this StructureAbout this Structure

2PD7 is a Single protein structure of sequence from Neurospora crassa with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Conformational switching in the fungal light sensor Vivid., Zoltowski BD, Schwerdtfeger C, Widom J, Loros JJ, Bilwes AM, Dunlap JC, Crane BR, Science. 2007 May 18;316(5827):1054-7. PMID:17510367

Page seeded by OCA on Thu Feb 21 18:28:24 2008

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

OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The Neurospora crassa photoreceptor Vivid tunes blue-light responses and, modulates gating of the circadian clock. Crystal structures of dark-state, and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim, domain with an unusual N-terminal cap region and a loop insertion that, accommodates the flavin cofactor. Photoinduced formation of a, cystein-flavin adduct drives flavin protonation to induce an N-terminal, conformational change. A cysteine-to-serine substitution remote from the, flavin adenine dinucleotide binding site decouples conformational, switching from the flavin photocycle and prevents Vivid from sending, signals in Neurospora. Key elements of this activation mechanism are, conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).
+The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 (FKF1).
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Neurospora crassa]]
 [[Category: Single protein]]
-[[Category: Bilwes, A.M.]]
+[[Category: Bilwes, A M.]]
-[[Category: Crane, B.R.]]
+[[Category: Crane, B R.]]
-[[Category: Zoltowski, B.D.]]
+[[Category: Zoltowski, B D.]]
 [[Category: FAD]]
 [[Category: lov domain; flavin; photoreceptor; circadian clock]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:01:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:24 2008''