7ygw | pdb_00007ygw

Crystal structure of the Zn2+-bound EFhd1/Swiprosin-2

spinqualitylabelsall models 7ygw, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ygw is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: GOL, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EFHD1_MOUSE Acts as a calcium sensor for mitochondrial flash (mitoflash) activation, an event characterized by stochastic bursts of superoxide production (By similarity). May play a role in neuronal differentiation (PubMed:16336229).[UniProtKB:Q9BUP0] Publication Abstract from PubMed EF-hand proteins, which contain a Ca(2+)-binding EF-hand motif, are involved in regulating diverse cellular functions. Ca(2+) binding induces conformational changes that modulate the activities of EF-hand proteins. Moreover, these proteins occasionally modify their activities by coordinating metals other than Ca(2+), including Mg(2+), Pb(2+) and Zn(2+), within their EF-hands. EFhd1 and EFhd2 are homologous EF-hand proteins with similar structures. Although separately localized within cells, both are actin-binding proteins that modulate F-actin rearrangement through Ca(2+)-independent actin-binding and Ca(2+)-dependent actin-bundling activity. Although Ca(2+) is known to affect the activities of EFhd1 and EFhd2, it is not known whether their actin-related activities are affected by other metals. Here, the crystal structures of the EFhd1 and EFhd2 core domains coordinating Zn(2+) ions within their EF-hands are reported. The presence of Zn(2+) within EFhd1 and EFhd2 was confirmed by analyzing anomalous signals and the difference between anomalous signals using data collected at the peak positions as well as low-energy remote positions at the Zn K-edge. EFhd1 and EFhd2 were also found to exhibit Zn(2+)-independent actin-binding and Zn(2+)-dependent actin-bundling activity. This suggests the actin-related activities of EFhd1 and EFhd2 could be regulated by Zn(2+) as well as Ca(2+). Structural and biochemical insights into Zn(2+)-bound EF-hand proteins, EFhd1 and EFhd2.,Mun SA, Park J, Kang JY, Park T, Jin M, Yang J, Eom SH IUCrJ. 2023 Mar 1;10(Pt 2):233-245. doi: 10.1107/S2052252523001501. PMID:36862489 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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