[NMR paper] Characterization of red/green cyanobacteriochrome NpR6012g4 by solution NMR spectroscopy: a hydrophobic pocket for the C15-E,anti chromophore in the photoproduct.
Characterization of red/green cyanobacteriochrome NpR6012g4 by solution NMR spectroscopy: a hydrophobic pocket for the C15-E,anti chromophore in the photoproduct.
Related ArticlesCharacterization of red/green cyanobacteriochrome NpR6012g4 by solution NMR spectroscopy: a hydrophobic pocket for the C15-E,anti chromophore in the photoproduct.
Abstract
Cyanobacteriochromes (CBCRs) are cyanobacterial photosensory proteins distantly related to phytochromes. Like phytochromes, CBCRs reversibly photoconvert between a dark-stable state and a photoproduct via photoisomerization of the 15,16-double bond of their linear tetrapyrrole (bilin) chromophores. CBCRs provide cyanobacteria with complete coverage of the visible spectrum and near ultraviolet. One CBCR subfamily, the canonical red/green CBCRs typified by AnPixJg2 and NpR6012g4, can function as sensors of light color or intensity due to their great variation in photoproduct stability. The mechanistic basis for detection of green light by the photoproduct state in this subfamily has proven a challenging research topic, with competing hydration and trapped-twist models proposed. Here, we use 13C-edited and 15N-edited 1H-1H NOESY solution NMR spectroscopy to probe changes in chromophore configuration and protein-chromophore interactions in the NpR6012g4 photocycle. Our results confirm a C15-Z,anti configuration for the red-absorbing dark state and reveal a C15-E,anti configuration for the green-absorbing photoproduct. The photoactive chromophore D-ring is located in a hydrophobic environment in the photoproduct, surrounded by both aliphatic and aromatic residues. Characterization of variant proteins demonstrates that no aliphatic residue is essential for photoproduct tuning. Taken together, our results support the trapped-twist model over the hydration model for the red/green photocycle of NpR6012g4.
PMID: 25989712 [PubMed - as supplied by publisher]
StructuralBasis of the Green–Blue Color Switchingin Proteorhodopsin as Determined by NMR Spectroscopy
StructuralBasis of the Green–Blue Color Switchingin Proteorhodopsin as Determined by NMR Spectroscopy
Jiafei Mao, Nhu-Nguyen Do, Frank Scholz, Lenica Reggie, Michaela Mehler, Andrea Lakatos, Yean-Sin Ong, Sandra J. Ullrich, Lynda J. Brown, Richard C. D. Brown, Johanna Becker-Baldus, Josef Wachtveitl and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja5097946/20141204/images/medium/ja-2014-097946_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja5097946...
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[NMR paper] Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
J Biochem. 2013 Oct 4;
Authors: Yuasa N, Koyama T, Subedi GP, Yamaguchi Y, Matsushita M, Fujita-Yamaguchi Y
Abstract
T-antigen (Gal?1-3GalNAc?-1-Ser/Thr), also known as...
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[NMR paper] NMR-assisted computational studies of peptidomimetic inhibitors bound in the hydrophobic pocket of HIV-1 glycoprotein 41.
NMR-assisted computational studies of peptidomimetic inhibitors bound in the hydrophobic pocket of HIV-1 glycoprotein 41.
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J Comput Aided Mol Des. 2013 Jul 27;
Authors: Gochin M, Whitby LR, Phillips AH, Boger DL
Abstract
Due to the inherently flexible nature of a protein-protein interaction surface, it is difficult both to inhibit the association with a small molecule, and to predict how it might bind to...
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Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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[NMR paper] Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytoch
Heteronuclear solution-state NMR studies of the chromophore in cyanobacterial phytochrome Cph1.
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Biochemistry. 2005 Jun 14;44(23):8244-50
Authors: Strauss HM, Hughes J, Schmieder P
Precise structural information regarding the chromophore binding pocket is essential for an understanding of photochromicity and photoconversion in phytochrome photoreceptors. To this end, we are studying the 59 kDa N-terminal module of the cyanobacterial...
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[NMR paper] The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a compa
The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a comparison with the structure of microcystin-LR.
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Eur J Biochem. 1998 Dec 1;258(2):301-12
Authors: Trogen GB, Edlund U, Larsson G, Sethson I
The microcystin-RR structures are compared with the structures of microcystin-LR in solution as well as in the crystal structure of the complex with protein phosphatase. The gross...
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[NMR paper] Secondary structure in solution of the hydrophobic protein of soybean (HPS) as reveal
Secondary structure in solution of the hydrophobic protein of soybean (HPS) as revealed by 1H NMR.
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J Biomol Struct Dyn. 1995 Apr;12(5):1009-22
Authors: Sodano P, Ptak M
COSY, TOCSY and NOESY experiments have been used to assign sequentially the 1H 500 MHz NMR spectra of the Hydrophobic Protein of Soybean (HPS). Spin systems identification combined with sequential assignment allowed to identify the proton resonances of this 80...
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[NMR paper] Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
Two-dimensional NMR characterization of the deoxymyoglobin heme pocket.
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Biochemistry. 1994 Sep 13;33(36):10934-43
Authors: Busse SC, Jue T
Traditionally, assigning the heme protein resonances has relied heavily on the comparison of spectra arising from protein reconstituted with specifically deuterated hemes and the native form. Such an approach can identify tentatively the broad, overlapping signals in the Fe(II) high-spin heme protein spectra. Although...
Characterization of red/green cyanobacteriochrome NpR6012g4 by solution NMR spectroscopy: a hydrophobic pocket for the C15-E,anti chromophore in the photoproduct.
Linear Mode
