7psd | pdb_00007psd

Structure of CtAtm1(E603Q) in the inward-facing open conformation

spinqualitylabelsall models 7psd, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7psd is a 2 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SBE6_CHATD Publication Abstract from PubMed In eukaryotes, iron-sulfur clusters are essential cofactors for numerous physiological processes, but these clusters are primarily biosynthesized in mitochondria. Previous studies suggest mitochondrial ABCB7-type exporters are involved in maturation of cytosolic iron-sulfur proteins. However, the molecular mechanism for how the ABCB7-type exporters participate in this process remains elusive. Here, we report a series of cryo-electron microscopy structures of a eukaryotic homolog of human ABCB7, CtAtm1, determined at average resolutions ranging from 2.8 to 3.2 A, complemented by functional characterization and molecular docking in silico. We propose that CtAtm1 accepts delivery from glutathione-complexed iron-sulfur clusters. A partially occluded state links cargo-binding to residues at the mitochondrial matrix interface that line a positively charged cavity, while the binding region becomes internalized and is partially divided in an early occluded state. Collectively, our findings substantially increase the understanding of the transport mechanism of eukaryotic ABCB7-type proteins. Structures of Atm1 provide insight into [2Fe-2S] cluster export from mitochondria.,Li P, Hendricks AL, Wang Y, Villones RLE, Lindkvist-Petersson K, Meloni G, Cowan JA, Wang K, Gourdon P Nat Commun. 2022 Jul 27;13(1):4339. doi: 10.1038/s41467-022-32006-8. PMID:35896548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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