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3AZC

Crystal structure of the soluble part of cytochrome b6f complex iron-sulfur subunit from Thermosynechococcus elongatus BP-1

Summary for 3AZC
Entry DOI10.2210/pdb3azc/pdb
DescriptorCytochrome b6-f complex iron-sulfur subunit, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
Functional Keywordsrieske, cytochrome b6f complex, thermosynechococcus elongatus, photosynthesis, electron transport, thylakoid membrane, oxidoreductase
Biological sourceThermosynechococcus elongatus
Cellular locationCellular thylakoid membrane; Single-pass membrane protein (By similarity): P0C8N8
Total number of polymer chains1
Total formula weight14821.38
Authors
Veit, S.,Takeda, K.,Tsunoyama, Y.,Roegner, M.,Miki, K. (deposition date: 2011-05-23, release date: 2012-05-23, Last modification date: 2024-11-20)
Primary citationVeit, S.,Takeda, K.,Tsunoyama, Y.,Rexroth, D.,Rogner, M.,Miki, K.
Structure of a thermophilic cyanobacterial b(6)f-type Rieske protein
Acta Crystallogr.,Sect.D, 68:1400-1408, 2012
Cited by
PubMed Abstract: The `Rieske protein' PetC is one of the key subunits of the cytochrome b(6)f complex. Its Rieske-type [2Fe-2S] cluster participates in the photosynthetic electron-transport chain. Overexpression and careful structure analysis at 2.0 Å resolution of the extrinsic soluble domain of PetC from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 enabled in-depth spectroscopic and structural characterization and suggested novel structural features. In particular, both the protein structure and the positions of the internal water molecules unexpectedly showed a higher similarity to eukaryotic PetCs than to other prokaryotic PetCs. The structure also revealed a deep pocket on the PetC surface which is oriented towards the membrane surface in the whole complex. Its surface properties suggest a binding site for a hydrophobic compound and the complete conservation of the pocket-forming residues in all known PetC sequences indicates the functional importance of this pocket in the cytochrome b(6)f complex.
PubMed: 22993094
DOI: 10.1107/S0907444912034129
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

238895

數據於2025-07-16公開中

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