7op8 | pdb_00007op8

Cryo-EM structure of P5B-ATPase E2Pinhibit

spinqualitylabelsall models 7op8, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7op8 is a 1 chain structure with sequence from Chatd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BEF, MG Gene: CTHT_0028100 (CHATD) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed In human cells, P5B-ATPases execute the active export of physiologically important polyamines such as spermine from lysosomes to the cytosol, a function linked to a palette of disorders. Yet, the overall shape of P5B-ATPases and the mechanisms of polyamine recognition, uptake and transport remain elusive. Here we describe a series of cryo-electron microscopy structures of a yeast homolog of human ATP13A2-5, Ypk9, determined at resolutions reaching 3.4 A, and depicting three separate transport cycle intermediates, including spermine-bound conformations. Surprisingly, in the absence of cargo, Ypk9 rests in a phosphorylated conformation auto-inhibited by the N-terminus. Spermine uptake is accomplished through an electronegative cleft lined by transmembrane segments 2, 4 and 6. Despite the dramatically different nature of the transported cargo, these findings pinpoint shared principles of transport and regulation among the evolutionary related P4-, P5A- and P5B-ATPases. The data also provide a framework for analysis of associated maladies, such as Parkinson's disease. Structure and transport mechanism of P5B-ATPases.,Li P, Wang K, Salustros N, Gronberg C, Gourdon P Nat Commun. 2021 Jun 25;12(1):3973. doi: 10.1038/s41467-021-24148-y. PMID:34172751 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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