[English] 日本語
Yorodumi
- PDB-2n77: NMR solution structure of a complex of PEP-19 bound to the C-doma... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2n77
TitleNMR solution structure of a complex of PEP-19 bound to the C-domain of apo calmodulin
Components
  • Calmodulin
  • Purkinje cell protein 4
KeywordsSIGNALING PROTEIN / intrinsically disordered / structural transition
Function / homology
Function and homology information


: / : / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / regulation of synaptic vesicle endocytosis / Reduction of cytosolic Ca++ levels ...: / : / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / Calmodulin induced events / regulation of synaptic vesicle endocytosis / Reduction of cytosolic Ca++ levels / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / regulation of synaptic vesicle exocytosis / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / positive regulation of cyclic-nucleotide phosphodiesterase activity / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / response to corticosterone / autophagosome membrane docking / mitochondrion-endoplasmic reticulum membrane tethering / CLEC7A (Dectin-1) induces NFAT activation / Activation of RAC1 downstream of NMDARs / regulation of cardiac muscle cell action potential / positive regulation of DNA binding / positive regulation of ryanodine-sensitive calcium-release channel activity / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Synthesis of IP3 and IP4 in the cytosol / negative regulation of peptidyl-threonine phosphorylation / Negative regulation of NMDA receptor-mediated neuronal transmission / Phase 0 - rapid depolarisation / Unblocking of NMDA receptors, glutamate binding and activation / negative regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / RHO GTPases activate PAKs / Ion transport by P-type ATPases / : / Uptake and function of anthrax toxins / Long-term potentiation / adenylate cyclase binding / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / catalytic complex / DARPP-32 events / detection of calcium ion / regulation of cardiac muscle contraction / Smooth Muscle Contraction / regulation of ryanodine-sensitive calcium-release channel activity / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / cellular response to interferon-beta / phosphatidylinositol 3-kinase binding / eNOS activation / Protein methylation / voltage-gated potassium channel complex / activation of adenylate cyclase activity / enzyme regulator activity / Activation of AMPK downstream of NMDARs / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / Ion homeostasis / : / titin binding / positive regulation of protein autophosphorylation / regulation of calcium-mediated signaling / sperm midpiece / calcium channel complex / nitric-oxide synthase regulator activity / positive regulation of neuron differentiation / substantia nigra development / adenylate cyclase activator activity / response to amphetamine / Ras activation upon Ca2+ influx through NMDA receptor / regulation of heart rate / sarcomere / FCERI mediated Ca+2 mobilization / protein serine/threonine kinase activator activity / FCGR3A-mediated IL10 synthesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of nitric-oxide synthase activity / VEGFR2 mediated vascular permeability / regulation of cytokinesis / VEGFR2 mediated cell proliferation / positive regulation of peptidyl-threonine phosphorylation / spindle microtubule / Translocation of SLC2A4 (GLUT4) to the plasma membrane / mitochondrial membrane / positive regulation of receptor signaling pathway via JAK-STAT / RAF activation / Transcriptional activation of mitochondrial biogenesis / positive regulation of protein serine/threonine kinase activity / Stimuli-sensing channels / cellular response to type II interferon / spindle pole
Similarity search - Function
: / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair
Similarity search - Domain/homology
Calmodulin-1 / Calmodulin regulator protein PCP4 / Calmodulin-3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailsclosest to the average, model1
AuthorsWang, X. / Putkey, J.A.
CitationJournal: Nat Commun / Year: 2016
Title: PEP-19 modulates calcium binding to calmodulin by electrostatic steering.
Authors: Wang, X. / Putkey, J.A.
History
DepositionSep 4, 2015Deposition site: BMRB / Processing site: RCSB
Revision 1.0Nov 30, 2016Provider: repository / Type: Initial release
Revision 1.1Dec 7, 2016Group: Database references
Revision 1.2Aug 18, 2021Group: Data collection / Database references / Experimental preparation
Category: database_2 / pdbx_nmr_exptl_sample ...database_2 / pdbx_nmr_exptl_sample / pdbx_nmr_sample_details / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_sample_details.contents / _pdbx_nmr_sample_details.label / _pdbx_nmr_sample_details.type / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.3May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Calmodulin
B: Purkinje cell protein 4


Theoretical massNumber of molelcules
Total (without water)15,2032
Polymers15,2032
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 300structures with the lowest energy
RepresentativeModel #1closest to the average

-
Components

#1: Protein Calmodulin / CaM


Mass: 8416.203 Da / Num. of mol.: 1 / Fragment: EF-hand domains 3 and 4, residues 77-149
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII
Production host: Escherichia coli (E. coli) / Strain (production host): K12 / Variant (production host): BL21(DE3)pLysS / References: UniProt: P62158, UniProt: P0DP23*PLUS
#2: Protein Purkinje cell protein 4 / Brain-specific antigen PCP-4 / Brain-specific polypeptide PEP-19


Mass: 6786.422 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PCP4, PEP19 / Production host: Escherichia coli (E. coli) / Strain (production host): K12 / Variant (production host): BL21(DE3)pLysS / References: UniProt: P48539

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D HNCA
1313D HN(CO)CA
1413D HN(CA)CB
1513D CBCA(CO)NH
1613D HNCO
1713D C(CO)NH
1813D H(CCO)NH
1913D HBHA(CO)NH
11013D 1H-15N NOESY
11132D 1H-13C HSQC
11233D (H)CCH-TOCSY
11333D (H)CCH-COSY
11433D CCH-TOCSY
11533D 1H-13C NOESY aliphatic
11633D F1--filtered, F3-edited NOESY-HSQC
11722D 1H-15N HSQC
11823D HNCA
11923D HN(CO)CA
12023D CBCA(CO)NH
12123D HN(CA)CB
12223D HNCO
12323D 1H-15N NOESY
12423D C(CO)NH
12523D H(CCO)NH
12623D HBHA(CO)NH
12742D 1H-13C HSQC
12842D 1H-13C HSQC aromatic
12943D (H)CCH-TOCSY
13043D (H)CCH-COSY
13143D CCH-TOCSY
13243D 1H-13C NOESY aliphatic
1334D F1--filtered, F3-edited NOESY-HSQC
1345IPAP 1H-15N HSQC

-
Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution10.8 mM [U-100% 13C; U-100% 15N] C-CaM, 1.0 mM PEP_19, 100 mM potassium chloride, 5 mM [U-2H] EDTA, 10 uM [U-2H] DSS, 10 mM [U-2H] imidazole, 95% H2O/5% D2Osample_195% H2O/5% D2O
solution20.8 mM [U-100% 13C; U-100% 15N] PEP_19, 1.0 mM C-CaM, 100 mM potassium chloride, 5 mM [U-2H] EDTA, 10 uM [U-2H] DSS, 10 mM [U-2H] imidazole, 95% H2O/5% D2Osample_295% H2O/5% D2O
solution30.8 mM [U-100% 13C; U-100% 15N] C-CaM, 1.0 mM PEP_19, 100 mM potassium chloride, 5 mM [U-2H] EDTA, 10 uM [U-2H] DSS, 10 mM [U-2H] imidazole, 100% D2Osample_3100% D2O
solution40.8 mM [U-100% 13C; U-100% 15N] PEP, 1.0 mM C-CaM, 100 mM potassium chloride, 5 mM [U-2H] EDTA, 10 uM [U-2H] DSS, 10 mM [U-2H] imidazole, 100% D2Osample_4100% D2O
solution50.5 mM [U-99% 15N] C-CaM, 1.0 mM PEP_19, 5.0 mM [U-2H] EDTA, 5% C12E5 PEG, 100 mM potassium chloride, 10 mM [U-2H] imidazole, 95% H2O/5% D2Osample_595% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.8 mMC-CaM[U-100% 13C; U-100% 15N]1
1.0 mMPEP_19natural abundance1
100 mMpotassium chloridenatural abundance1
5 mMEDTA[U-2H]1
10 uMDSS[U-2H]1
10 mMimidazole[U-2H]1
0.8 mMPEP_19[U-100% 13C; U-100% 15N]2
1.0 mMC-CaMnatural abundance2
100 mMpotassium chloridenatural abundance2
5 mMEDTA[U-2H]2
10 uMDSS[U-2H]2
10 mMimidazole[U-2H]2
0.8 mMC-CaM[U-100% 13C; U-100% 15N]3
1.0 mMPEP_19natural abundance3
100 mMpotassium chloridenatural abundance3
5 mMEDTA[U-2H]3
10 uMDSS[U-2H]3
10 mMimidazole[U-2H]3
0.8 mMPEP-19[U-100% 13C; U-100% 15N]4
1.0 mMC-CaMnatural abundance4
100 mMpotassium chloridenatural abundance4
5 mMEDTA[U-2H]4
10 uMDSS[U-2H]4
10 mMimidazole[U-2H]4
0.5 mMC-CaM[U-99% 15N]5
1 mMPEP_19natural abundance5
5 mMEDTA[U-2H]5
5 %C12E5 PEGnatural abundance5
100 mMpotassium chloridenatural abundance5
10 mMimidazole[U-2H]5
Sample conditionsIonic strength: 0.1 / pH: 6.3 / Pressure: ambient / Temperature: 298 K

-
NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

-
Processing

NMR software
NameVersionDeveloperClassification
XPLOR-NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
FelixAccelrys Software Inc.data analysis
FelixAccelrys Software Inc.processing
TopSpin2.1Bruker Biospincollection
RefinementMethod: simulated annealing / Software ordinal: 1
NMR constraintsNOE constraints total: 1917 / Hydrogen bond constraints total count: 98 / Protein other angle constraints total count: 0
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 300 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum upper distance constraint violation: 0 Å

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more