7s9y | pdb_00007s9y

Helicobacter Hepaticus CcsBA Open Conformation

spinqualitylabelsall models 7s9y, resolution 3.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7s9y is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEB, PTY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Although the individual structures and respiratory functions of cytochromes are well studied, the structural basis for their assembly, including transport of heme for attachment, are unknown. We describe cryo-electron microscopy (cryo-EM) structures of CcsBA, a bifunctional heme transporter and cytochrome c (cyt c) synthase. Models built from the cryo-EM densities show that CcsBA is trapped with heme in two conformations, herein termed the closed and open states. The closed state has heme located solely at a transmembrane (TM) site, with a large periplasmic domain oriented such that access of heme to the cytochrome acceptor is denied. The open conformation contains two heme moieties, one in the TM-heme site and another in an external site (P-heme site). The presence of heme in the periplasmic site at the base of a chamber induces a large conformational shift that exposes the heme for reaction with apocytochrome c (apocyt c). Consistent with these structures, in vivo and in vitro cyt c synthase studies suggest a mechanism for transfer of the periplasmic heme to cytochrome. Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.,Mendez DL, Lowder EP, Tillman DE, Sutherland MC, Collier AL, Rau MJ, Fitzpatrick JAJ, Kranz RG Nat Chem Biol. 2022 Jan;18(1):101-108. doi: 10.1038/s41589-021-00935-y. Epub 2021, Dec 20. PMID:34931065 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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