(Q27646817)

English

Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion

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scholarly article

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Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion (English)

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crystal structure

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author name string

Xiaojing Yang

1

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Emina A Stojkovic

2

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Jane Kuk

3

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Keith Moffat

4

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language of work or name

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publication date

24 July 2007

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Proceedings of the National Academy of Sciences of the United States of America

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104

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30

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12571-6

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High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution

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REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use

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Likelihood-enhanced fast rotation functions

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Maximum-likelihood density modification

1 reference

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2 references

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1 reference

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29 September 2017

Phytochrome structure and signaling mechanisms.

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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2 June 2018

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1 reference

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Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore

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A new type of bacteriophytochrome acts in tandem with a classical bacteriophytochrome to control the antennae synthesis in Rhodopseudomonas palustris

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A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome

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Light-dependent dimerisation in the N-terminal sensory module of cyanobacterial phytochrome 1.

1 reference

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Protein conformational changes of Agrobacterium phytochrome Agp1 during chromophore assembly and photoconversion.

1 reference

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Sterically locked synthetic bilin derivatives and phytochrome Agp1 from Agrobacterium tumefaciens form photoinsensitive Pr- and Pfr-like adducts.

1 reference

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Biochemical and spectroscopic characterization of the bacterial phytochrome of Pseudomonas aeruginosa

1 reference

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Highly conserved residues Asp-197 and His-250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation.

1 reference

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1 reference

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

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Analysis of the Topology of the Chromophore Binding Pocket of Phytochromes by Variation of the Chromophore Substitution Pattern

1 reference

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12 December 2020

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Identifiers

10.1073/PNAS.0701737104

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2007PNAS..10412571Y

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