Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.

3-D images of marine mammal Opn4 proteins (teal) were aligned with squid Rh1 (green) to determine relative positions of helices and residues. (A) squid rhodopsin (Protein Data Bank accession number 2Z73) showing the relative position of the ten nonconservative amino acid substitutions from Fig 3 . A...

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Main Authors: Jeffry I. Fasick (3624569), Haya Algrain (11570761), Courtland Samuels (11570764), Padmanabhan Mahadevan (475388), Lorian E. Schweikert (3624572), Zaid J. Naffaa (11570767), Phyllis R. Robinson (204369)
Format: Still Image
Language:unknown
Published: 2021
Subjects:
Online Access:https://doi.org/10.1371/journal.pone.0257436.g004
id ftsmithonian:oai:figshare.com:article/16820467
record_format openpolar
spelling ftsmithonian:oai:figshare.com:article/16820467 2023-05-15T18:43:22+02:00 Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions. Jeffry I. Fasick (3624569) Haya Algrain (11570761) Courtland Samuels (11570764) Padmanabhan Mahadevan (475388) Lorian E. Schweikert (3624572) Zaid J. Naffaa (11570767) Phyllis R. Robinson (204369) 2021-10-15T17:31:17Z https://doi.org/10.1371/journal.pone.0257436.g004 unknown https://figshare.com/articles/figure/Structural_modeling_of_marine_mammal_melanopsin_Opn4_spectral_tuning_amino_acid_positions_/16820467 doi:10.1371/journal.pone.0257436.g004 CC BY 4.0 CC-BY Biochemistry Cell Biology Molecular Biology Neuroscience Evolutionary Biology Ecology Virology Environmental Sciences not elsewhere classified water &# 8217 serve light detection retinal ganglion cells carboxyl terminal domain available light spectra marine mammal rhodopsins thus longer mydriasis extended pupillary constriction amino acid substitutions marine mammal species div >< p marine mammals may marine mammals pupil constriction mydriasis occurs identify substitutions given species values tuned values relative terrestrial counterparts terrestrial controls spectral tuning spectral sensitivity solar irradiance significant change rod retina rod monochromacy results suggest results show previous work prevent photobleaching orders sirenia likely involved infraorder cetacea highly photosensitive foraging depths deactivation kinetics condition known cdna sequences absorbance maxima Image Figure 2021 ftsmithonian https://doi.org/10.1371/journal.pone.0257436.g004 2021-12-20T00:06:09Z 3-D images of marine mammal Opn4 proteins (teal) were aligned with squid Rh1 (green) to determine relative positions of helices and residues. (A) squid rhodopsin (Protein Data Bank accession number 2Z73) showing the relative position of the ten nonconservative amino acid substitutions from Fig 3 . A proposed protonated Schiff base counterion (Glu214) [ 77 – 79 ] is shown in orange. Panels B-D highlight nonconservative amino acids potentially involved in spectral tuning and their relative predicted distance to the retinal Schiff base lysine (red) terminal NZ atom or the β-ionone ring of the chromophore (yellow): (B) manatee Thr123 (9.5 Å); (C) Yangtze river dolphin Thr128 (11.8 Å); and (D) Weddell seal Ala311 (9.3 Å); Weddell seal and walrus Thr315 (11.2 Å). Opn4 numbering is from mouse. Still Image Weddell Seal walrus* Unknown Weddell
institution Open Polar
collection Unknown
op_collection_id ftsmithonian
language unknown
topic Biochemistry
Cell Biology
Molecular Biology
Neuroscience
Evolutionary Biology
Ecology
Virology
Environmental Sciences not elsewhere classified
water &# 8217
serve light detection
retinal ganglion cells
carboxyl terminal domain
available light spectra
marine mammal rhodopsins
thus longer mydriasis
extended pupillary constriction
amino acid substitutions
marine mammal species
div >< p
marine mammals may
marine mammals
pupil constriction
mydriasis occurs
identify substitutions
given species
values tuned
values relative
terrestrial counterparts
terrestrial controls
spectral tuning
spectral sensitivity
solar irradiance
significant change
rod retina
rod monochromacy
results suggest
results show
previous work
prevent photobleaching
orders sirenia
likely involved
infraorder cetacea
highly photosensitive
foraging depths
deactivation kinetics
condition known
cdna sequences
absorbance maxima
spellingShingle Biochemistry
Cell Biology
Molecular Biology
Neuroscience
Evolutionary Biology
Ecology
Virology
Environmental Sciences not elsewhere classified
water &# 8217
serve light detection
retinal ganglion cells
carboxyl terminal domain
available light spectra
marine mammal rhodopsins
thus longer mydriasis
extended pupillary constriction
amino acid substitutions
marine mammal species
div >< p
marine mammals may
marine mammals
pupil constriction
mydriasis occurs
identify substitutions
given species
values tuned
values relative
terrestrial counterparts
terrestrial controls
spectral tuning
spectral sensitivity
solar irradiance
significant change
rod retina
rod monochromacy
results suggest
results show
previous work
prevent photobleaching
orders sirenia
likely involved
infraorder cetacea
highly photosensitive
foraging depths
deactivation kinetics
condition known
cdna sequences
absorbance maxima
Jeffry I. Fasick (3624569)
Haya Algrain (11570761)
Courtland Samuels (11570764)
Padmanabhan Mahadevan (475388)
Lorian E. Schweikert (3624572)
Zaid J. Naffaa (11570767)
Phyllis R. Robinson (204369)
Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
topic_facet Biochemistry
Cell Biology
Molecular Biology
Neuroscience
Evolutionary Biology
Ecology
Virology
Environmental Sciences not elsewhere classified
water &# 8217
serve light detection
retinal ganglion cells
carboxyl terminal domain
available light spectra
marine mammal rhodopsins
thus longer mydriasis
extended pupillary constriction
amino acid substitutions
marine mammal species
div >< p
marine mammals may
marine mammals
pupil constriction
mydriasis occurs
identify substitutions
given species
values tuned
values relative
terrestrial counterparts
terrestrial controls
spectral tuning
spectral sensitivity
solar irradiance
significant change
rod retina
rod monochromacy
results suggest
results show
previous work
prevent photobleaching
orders sirenia
likely involved
infraorder cetacea
highly photosensitive
foraging depths
deactivation kinetics
condition known
cdna sequences
absorbance maxima
description 3-D images of marine mammal Opn4 proteins (teal) were aligned with squid Rh1 (green) to determine relative positions of helices and residues. (A) squid rhodopsin (Protein Data Bank accession number 2Z73) showing the relative position of the ten nonconservative amino acid substitutions from Fig 3 . A proposed protonated Schiff base counterion (Glu214) [ 77 – 79 ] is shown in orange. Panels B-D highlight nonconservative amino acids potentially involved in spectral tuning and their relative predicted distance to the retinal Schiff base lysine (red) terminal NZ atom or the β-ionone ring of the chromophore (yellow): (B) manatee Thr123 (9.5 Å); (C) Yangtze river dolphin Thr128 (11.8 Å); and (D) Weddell seal Ala311 (9.3 Å); Weddell seal and walrus Thr315 (11.2 Å). Opn4 numbering is from mouse.
format Still Image
author Jeffry I. Fasick (3624569)
Haya Algrain (11570761)
Courtland Samuels (11570764)
Padmanabhan Mahadevan (475388)
Lorian E. Schweikert (3624572)
Zaid J. Naffaa (11570767)
Phyllis R. Robinson (204369)
author_facet Jeffry I. Fasick (3624569)
Haya Algrain (11570761)
Courtland Samuels (11570764)
Padmanabhan Mahadevan (475388)
Lorian E. Schweikert (3624572)
Zaid J. Naffaa (11570767)
Phyllis R. Robinson (204369)
author_sort Jeffry I. Fasick (3624569)
title Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
title_short Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
title_full Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
title_fullStr Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
title_full_unstemmed Structural modeling of marine mammal melanopsin (Opn4) spectral tuning amino acid positions.
title_sort structural modeling of marine mammal melanopsin (opn4) spectral tuning amino acid positions.
publishDate 2021
url https://doi.org/10.1371/journal.pone.0257436.g004
geographic Weddell
geographic_facet Weddell
genre Weddell Seal
walrus*
genre_facet Weddell Seal
walrus*
op_relation https://figshare.com/articles/figure/Structural_modeling_of_marine_mammal_melanopsin_Opn4_spectral_tuning_amino_acid_positions_/16820467
doi:10.1371/journal.pone.0257436.g004
op_rights CC BY 4.0
op_rightsnorm CC-BY
op_doi https://doi.org/10.1371/journal.pone.0257436.g004
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