 |
PDBsum entry 5j3w
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
5j3w
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Signaling states of a short blue-Light photoreceptor protein ppsb1-Lov revealed from crystal structures and solution nmr spectroscopy.
|
|
|
Authors
|
|
K.Röllen,
J.Granzin,
V.Panwalkar,
V.Arinkin,
R.Rani,
R.Hartmann,
U.Krauss,
K.E.Jaeger,
D.Willbold,
R.Batra-Safferling.
|
|
|
Ref.
|
|
J Mol Biol, 2016,
428,
3721-3736.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Light-Oxygen-Voltage (LOV) domains represent the photo-responsive domains of
various blue-light photoreceptor proteins and are widely distributed in plants,
algae, fungi, and bacteria. Here, we report the dark-state crystal structure of
PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida that is
remarkably different from our previously published "fully
light-adapted" structure [1]. A direct comparison of the two structures
provides insight into the light-activated signaling mechanism. Major structural
differences involve a~11Å movement of the C terminus in helix Jα, ~4Å
movement of Hβ-Iβ loop, disruption of hydrogen bonds in the dimer interface,
and a~29° rotation of chain-B relative to chain-A as compared to the
light-state dimer. Both crystal structures and solution NMR data are suggestive
of the key roles of a conserved glutamine Q116 and the N-cap region consisting
of A'α-Aβ loop and the A'α helix in controlling the light-activated
conformational changes. The activation mechanism proposed here for the PpSB1-LOV
supports a rotary switch mechanism and provides insights into the signal
propagation mechanism in naturally existing and artificial LOV-based,
two-component systems and regulators.
|
|
|
|
|
|
|
