Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Structural basis for ligh… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome

Artikel i vetenskaplig tidskrift
Författare N. C. Woitowich
A. S. Halavaty
P. Waltz
C. Kupitz
J. Valera
G. Tracy
K. D. Gallagher
Elin Claesson
T. Nakane
S. Pandey
G. Nelson
R. Tanaka
E. Nango
E. Mizohata
S. Owada
K. Tono
Y. Joti
A. C. Nugent
H. Patel
A. Mapara
J. Hopkins
P. Duong
D. Bizhga
S. E. Kovaleva
R. St Peter
C. N. Hernandez
W. B. Ozarowski
S. Roy-Chowdhuri
J. H. Yang
Petra Edlund
H. Takala
J. Ihalainen
J. Brayshaw
T. Norwood
I. Poudyal
P. Fromme
J. C. H. Spence
K. Moffat
Sebastian Westenhoff
M. Schmidt
E. A. Stojkovic
Publicerad i Iucrj
Volym 5
Nummer/häfte Part 5
Sidor 619-634
ISSN 2052-2525
Publiceringsår 2018
Publicerad vid Institutionen för kemi och molekylärbiologi
Sidor 619-634
Språk en
Länkar dx.doi.org/10.1107/s205225251801063...
Ämnesord phytochromes, photoreceptors, photosynthetic bacteria, myxobacteria, absorption spectra, photoactive yellow protein, chromophore-binding domain, fruiting body, formation, stigmatella-aurantiaca, unusual bacteriophytochrome, molecular replacement, signaling mechanism, photoconversion, crystallography, module, Chemistry, Crystallography, Materials Science, ates of america, v106, p6123, ates of america, v105, p14709, ates of america, v111, pe237
Ämneskategorier Kemi

Sammanfattning

Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruitingbody formation of this photomorphogenic bacterium. SaBphP1 lacks a conserved histidine (His) in the chromophore-binding domain that stabilizes the Pr state in the classical BphPs. Instead it contains a threonine (Thr), a feature that is restricted to several myxobacterial phytochromes and is not evolutionarily understood. SaBphP1 structures of the chromophore binding domain (CBD) and the complete photosensory core module (PCM) in wild-type and Thr-to-His mutant forms reveal details of the molecular mechanism of the Pr/Pfr transition associated with the physiological response of this myxobacterium to red light. Specifically, key structural differences in the CBD and PCM between the wild-type and the Thr-to-His mutant involve essential chromophore contacts with proximal amino acids, and point to how the photosignal is transduced through the rest of the protein, impacting the essential enzymatic activity in the photomorphogenic response of this myxobacterium.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?