5ypu

Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu MET72NLE WH2-motif peptide

spinqualitylabelsall models 5ypu, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ypu is a 4 chain structure with sequence from Mus musculus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ATP, CA, NLE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMed The structure of the actin filament is known at a resolution that has allowed the architecture of protein components to be unambiguously assigned. However, fully understanding the chemistry of the system requires higher resolution to identify the ions and water molecules involved in polymerization and ATP hydrolysis. Here, we find experimental evidence for the association of cations with the surfaces of G-actin in a 2.0-A resolution X-ray structure of actin bound to a Cordon-Bleu WH2 motif and in previously determined high-resolution X-ray structures. Three of four reoccurring divalent cation sites were stable during molecular dynamics (MD) simulations of the filament, suggesting that these sites may play a functional role in stabilizing the filament. We modeled the water coordination at the ATP-bound Mg(2+), which also proved to be stable during the MD simulations. Using this model of the filament with a hydrated ATP-bound Mg(2+), we compared the cumulative probability of an activated hydrolytic water molecule approaching the gamma-phosphorous of ATP, in comparison with G-actin, in the MD simulations. The cumulative probability increased in F-actin in line with the activation of actin's ATPase activity on polymerization. However, inclusion of the cations in the filament lowered cumulative probability, suggesting the rate of hydrolysis may be linked to filament flexibility. Together, these data extend the possible roles of Mg(2+) in polymerization and the mechanism of polymerization-induced activation of actin's ATPase activity. Structural evidence for the roles of divalent cations in actin polymerization and activation of ATP hydrolysis.,Scipion CPM, Ghoshdastider U, Ferrer FJ, Yuen TY, Wongsantichon J, Robinson RC Proc Natl Acad Sci U S A. 2018 Sep 25. pii: 1806394115. doi:, 10.1073/pnas.1806394115. PMID:30254171 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin 3D structures

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