7TE2

Crystal Structure of AerR from Rhodobacter capsulatus at 2.25 A.

Summary for 7TE2

• Entry DOI: 10.2210/pdb7te2/pdb
• Descriptor: AerR, COBALAMIN, HEXANE-1,6-DIOL, ... (5 entities in total)
• Functional Keywords: transcription, b12 binding, transcription regulator, photosynthesis, gene regulator
• Biological source: Rhodobacter capsulatus Y262
• Total number of polymer chains: 1
• Total formula weight: 24309.34

Authors

Dragnea, V.,Gonzalez-Gutierrez, G.,Bauer, C.E. (deposition date: 2022-01-04, release date: 2022-08-31, Last modification date: 2024-02-28)

Primary citation

Dragnea, V.,Gonzalez-Gutierrez, G.,Bauer, C.E.
Structural Analyses of CrtJ and Its B 12 -Binding Co-Regulators SAerR and LAerR from the Purple Photosynthetic Bacterium Rhodobacter capsulatus.
Microorganisms, 10:-, 2022

PubMed Abstract: Among purple photosynthetic bacteria, the transcription factor CrtJ is a major regulator of photosystem gene expression. Depending on growing conditions, CrtJ can function as an aerobic repressor or an anaerobic activator of photosystem genes. Recently, CrtJ's activity was shown to be modulated by two size variants of a B binding co-regulator called SAerR and LAerR in . The short form, SAerR, promotes CrtJ repression, while the longer variant, LAerR, converts CrtJ into an activator. In this study, we solved the crystal structure of SAerR at a 2.25 Å resolution. Hydroxycobalamin bound to SAerR is sandwiched between a 4-helix bundle cap, and a Rossman fold. This structure is similar to a AerR-like domain present in CarH from , which is a combined photoreceptor/transcription regulator. We also utilized AlphaFold software to predict structures for the LAerR, CrtJ, SAerR-CrtJ and LAerR-CrtJ co-complexes. These structures provide insights into the role of B and an LAerR N-terminal extension in regulating the activity of CrtJ.

PubMed: 35630357
DOI: 10.3390/microorganisms10050912

Experimental method

X-RAY DIFFRACTION (2.25 Å)