2byc
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2byc |SIZE=350|CAPTION= <scene name='initialview01'>2byc</scene>, resolution 1.90Å | |PDB= 2byc |SIZE=350|CAPTION= <scene name='initialview01'>2byc</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Fmn+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fmn+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2byc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byc OCA], [http://www.ebi.ac.uk/pdbsum/2byc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2byc RCSB]</span> | ||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: Tarutina, M.]] | [[Category: Tarutina, M.]] | ||
[[Category: Wu, Q.]] | [[Category: Wu, Q.]] | ||
| - | [[Category: FMN]] | ||
[[Category: blue light sensing]] | [[Category: blue light sensing]] | ||
[[Category: bluf]] | [[Category: bluf]] | ||
| Line 38: | Line 40: | ||
[[Category: signaling]] | [[Category: signaling]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:33 2008'' |
Revision as of 23:13, 30 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BLRB- A BLUF PROTEIN, DARK STATE STRUCTURE
Overview
Light is an essential environmental factor, and many species have evolved the capability to respond to it. Blue light is perceived through three flavin-containing photoreceptor families: cryptochromes, light-oxygen-voltage, and BLUF (sensor of blue light using flavin adenine dinucleotide, FAD) domain proteins. BLUF domains are present in various proteins from Bacteria and lower Eukarya. They are fully modular and can relay signals to structurally and functionally diverse output units, most of which are implicated in nucleotide metabolism. We present the high resolution crystal structure of the dark resting state of BlrB, a short BLUF domain-containing protein from Rhodobacter sphaeroides. The structure reveals a previously uncharacterized FAD-binding fold. Along with other lines of evidence, it suggests mechanistic aspects for the photocycle that is characterized by a red-shifted absorbance of the flavin. The isoalloxazine ring of FAD binds in a cleft between two helices, whereas the adenine ring points into the solvent. We propose that the adenine ring serves as a hook mediating the interaction with its effector/output domain. The structure suggests a unique photochemical signaling switch in which the absorption of light induces a structural change in the rim surrounding the hook, thereby changing the protein interface between BLUF and the output domain.
About this Structure
2BYC is a Single protein structure of sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
Reference
Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction., Jung A, Domratcheva T, Tarutina M, Wu Q, Ko WH, Shoeman RL, Gomelsky M, Gardner KH, Schlichting I, Proc Natl Acad Sci U S A. 2005 Aug 30;102(35):12350-5. Epub 2005 Aug 17. PMID:16107542
Page seeded by OCA on Mon Mar 31 02:13:33 2008
