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4HH1

Dark-state structure of AppA wild-type without the Cys-rich region from Rb. sphaeroides

Summary for 4HH1
Entry DOI10.2210/pdb4hh1/pdb
Related1YRX 2IYG 2IYI 4HH0 4HH2 4HH3
DescriptorAppA protein, FLAVIN MONONUCLEOTIDE (2 entities in total)
Functional Keywordsbluf domain, schic domain, photoreceptor, ppsr, flavoprotein, signaling protein
Biological sourceRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Total number of polymer chains2
Total formula weight88662.73
Authors
Winkler, A.,Heintz, U.,Lindner, R.,Reinstein, J.,Shoeman, R.,Schlichting, I. (deposition date: 2012-10-09, release date: 2013-06-05, Last modification date: 2024-02-28)
Primary citationWinkler, A.,Heintz, U.,Lindner, R.,Reinstein, J.,Shoeman, R.L.,Schlichting, I.
A ternary AppA-PpsR-DNA complex mediates light regulation of photosynthesis-related gene expression.
Nat.Struct.Mol.Biol., 20:859-867, 2013
Cited by
PubMed Abstract: The anoxygenic phototrophic bacterium Rhodobacter sphaeroides uses different energy sources, depending on environmental conditions including aerobic respiration or, in the absence of oxygen, photosynthesis. Photosynthetic genes are repressed at high oxygen tension, but at intermediate levels their partial expression prepares the bacterium for using light energy. Illumination, however, enhances repression under semiaerobic conditions. Here, we describe molecular details of two proteins mediating oxygen and light control of photosynthesis-gene expression: the light-sensing antirepressor AppA and the transcriptional repressor PpsR. Our crystal structures of both proteins and their complex and hydrogen/deuterium-exchange data show that light activation of AppA-PpsR2 affects the PpsR effector region within the complex. DNA binding studies demonstrate the formation of a light-sensitive ternary AppA-PpsR-DNA complex. We discuss implications of these results for regulation by light and oxygen, highlighting new insights into blue light-mediated signal transduction.
PubMed: 23728293
DOI: 10.1038/nsmb.2597
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.501 Å)
Structure validation

238268

数据于2025-07-02公开中

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