- PDB-7nxv: Crystal structure of the complex of DNase I/G-actin/PPP1R15A_582-621 -
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Basic information
Entry
Database: PDB / ID: 7nxv
Title
Crystal structure of the complex of DNase I/G-actin/PPP1R15A_582-621
Components
Actin, alpha skeletal muscle, intermediate form
Deoxyribonuclease-1
Protein phosphatase 1 regulatory subunit 15A
Keywords
HYDROLASE / hydrolase regulator / protein phosphatase 1 regulatory unit
Function / homology
Function and homology information
positive regulation of translational initiation in response to stress / positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation / regulation of translational initiation by eIF2 alpha dephosphorylation / regulation of neutrophil mediated cytotoxicity / zymogen granule / regulation of acute inflammatory response / positive regulation of peptidyl-serine dephosphorylation / protein phosphatase type 1 complex / deoxyribonuclease I / Response of EIF2AK1 (HRI) to heme deficiency ...positive regulation of translational initiation in response to stress / positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation / regulation of translational initiation by eIF2 alpha dephosphorylation / regulation of neutrophil mediated cytotoxicity / zymogen granule / regulation of acute inflammatory response / positive regulation of peptidyl-serine dephosphorylation / protein phosphatase type 1 complex / deoxyribonuclease I / Response of EIF2AK1 (HRI) to heme deficiency / negative regulation of protein dephosphorylation / protein localization to endoplasmic reticulum / neutrophil activation involved in immune response / protein phosphatase regulator activity / protein phosphatase 1 binding / deoxyribonuclease I activity / DNA catabolic process / cytoskeletal motor activator activity / negative regulation of phosphoprotein phosphatase activity / negative regulation of PERK-mediated unfolded protein response / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / protein phosphatase activator activity / filamentous actin / actin filament bundle / positive regulation of phosphoprotein phosphatase activity / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / response to endoplasmic reticulum stress / Downregulation of TGF-beta receptor signaling / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / nuclear envelope / actin binding / cell body / mitochondrial outer membrane / hydrolase activity / regulation of cell cycle / protein domain specific binding / apoptotic process / DNA damage response / calcium ion binding / positive regulation of gene expression / endoplasmic reticulum membrane / protein kinase binding / Golgi apparatus / magnesium ion binding / endoplasmic reticulum / mitochondrion / DNA binding / extracellular region / ATP binding / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function
Protein phosphatase 1, regulatory subunit 15A/B, C-terminal / Phosphatase-1 catalytic subunit binding region / Deoxyribonuclease I / Deoxyribonuclease I, active site / Deoxyribonuclease I, conservied site / Deoxyribonuclease I signature 2. / Deoxyribonuclease I signature 1. / deoxyribonuclease I / Endonuclease/exonuclease/phosphatase / Endonuclease/Exonuclease/phosphatase family ...Protein phosphatase 1, regulatory subunit 15A/B, C-terminal / Phosphatase-1 catalytic subunit binding region / Deoxyribonuclease I / Deoxyribonuclease I, active site / Deoxyribonuclease I, conservied site / Deoxyribonuclease I signature 2. / Deoxyribonuclease I signature 1. / deoxyribonuclease I / Endonuclease/exonuclease/phosphatase / Endonuclease/Exonuclease/phosphatase family / Endonuclease/exonuclease/phosphatase superfamily / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain Similarity search - Domain/homology
Journal: Nat Struct Mol Biol / Year: 2021 Title: Higher-order phosphatase-substrate contacts terminate the integrated stress response. Authors: Yahui Yan / Heather P Harding / David Ron / Abstract: Many regulatory PPP1R subunits join few catalytic PP1c subunits to mediate phosphoserine and phosphothreonine dephosphorylation in metazoans. Regulatory subunits engage the surface of PP1c, locally ...Many regulatory PPP1R subunits join few catalytic PP1c subunits to mediate phosphoserine and phosphothreonine dephosphorylation in metazoans. Regulatory subunits engage the surface of PP1c, locally affecting flexible access of the phosphopeptide to the active site. However, catalytic efficiency of holophosphatases towards their phosphoprotein substrates remains unexplained. Here we present a cryo-EM structure of the tripartite PP1c-PPP1R15A-G-actin holophosphatase that terminates signaling in the mammalian integrated stress response (ISR) in the pre-dephosphorylation complex with its substrate, translation initiation factor 2α (eIF2α). G-actin, whose essential role in eIF2α dephosphorylation is supported crystallographically, biochemically and genetically, aligns the catalytic and regulatory subunits, creating a composite surface that engages the N-terminal domain of eIF2α to position the distant phosphoserine-51 at the active site. Substrate residues that mediate affinity for the holophosphatase also make critical contacts with eIF2α kinases. Thus, a convergent process of higher-order substrate recognition specifies functionally antagonistic phosphorylation and dephosphorylation in the ISR.
Mass: 41862.613 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) / References: UniProt: P68135
#2: Protein
Deoxyribonuclease-1 / Deoxyribonuclease I / DNase I
Mass: 29092.574 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00639, deoxyribonuclease I
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Protein/peptide / Sugars , 2 types, 4 molecules CE
#3: Protein/peptide
Proteinphosphatase1regulatorysubunit15A / Growth arrest and DNA damage-inducible protein GADD34 / Myeloid differentiation primary response ...Growth arrest and DNA damage-inducible protein GADD34 / Myeloid differentiation primary response protein MyD116 homolog
Mass: 4761.417 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPP1R15A, GADD34 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: O75807
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