3azc | pdb_00003azc

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

spinqualitylabelsall models 3azc, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3azc is a 1 chain structure with sequence from Thermosynechococcus elongatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FES Gene: petC, tlr0959 (Thermosynechococcus elongatus) Activity: Plastoquinol--plastocyanin reductase, with EC number 1.10.99.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 A 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. Structure of a thermophilic cyanobacterial b(6)f-type Rieske protein.,Veit S, Takeda K, Tsunoyama Y, Rexroth D, Rogner M, Miki K Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1400-8. Epub 2012 Sep 18. PMID:22993094 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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