[English] 日本語
Yorodumi
- PDB-4bxu: Structure of Pex14 in complex with Pex5 LVxEF motif -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4bxu
TitleStructure of Pex14 in complex with Pex5 LVxEF motif
Components
  • PEROXISOMAL MEMBRANE PROTEIN PEX14
  • PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR
KeywordsPROTEIN TRANSPORT / TRANSLOCATION
Function / homology
Function and homology information


peroxisome transport along microtubule / protein import into peroxisome matrix, substrate release / protein import into peroxisome matrix, translocation / peroxisome membrane targeting sequence binding / protein import into peroxisome membrane / peroxisome targeting sequence binding / protein targeting to peroxisome / peroxisome matrix targeting signal-1 binding / peroxisomal importomer complex / microtubule anchoring ...peroxisome transport along microtubule / protein import into peroxisome matrix, substrate release / protein import into peroxisome matrix, translocation / peroxisome membrane targeting sequence binding / protein import into peroxisome membrane / peroxisome targeting sequence binding / protein targeting to peroxisome / peroxisome matrix targeting signal-1 binding / peroxisomal importomer complex / microtubule anchoring / protein import into peroxisome matrix, receptor recycling / protein import into peroxisome matrix / protein import into peroxisome matrix, docking / Class I peroxisomal membrane protein import / protein carrier chaperone / very long-chain fatty acid metabolic process / cerebral cortex neuron differentiation / peroxisome organization / cell development / pexophagy / positive regulation of multicellular organism growth / endoplasmic reticulum organization / mitochondrial membrane organization / peroxisomal membrane / neuromuscular process / beta-tubulin binding / fatty acid beta-oxidation / cerebral cortex cell migration / peroxisomal matrix / protein transmembrane transporter activity / negative regulation of protein-containing complex assembly / Pexophagy / negative regulation of protein binding / Peroxisomal protein import / protein tetramerization / neuron migration / negative regulation of DNA-binding transcription factor activity / fibrillar center / small GTPase binding / cellular response to reactive oxygen species / transcription corepressor activity / peroxisome / E3 ubiquitin ligases ubiquitinate target proteins / protein-macromolecule adaptor activity / microtubule binding / protein-containing complex assembly / signaling receptor binding / negative regulation of DNA-templated transcription / Golgi apparatus / enzyme binding / protein-containing complex / mitochondrion / identical protein binding / membrane / nucleus / cytoplasm / cytosol
Similarity search - Function
Peroxisome membrane anchor protein Pex14p, N-terminal / Peroxisomal membrane protein 14 / Pex14 N-terminal domain / PEX5/PEX5L / Tetratricopeptide repeat / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat ...Peroxisome membrane anchor protein Pex14p, N-terminal / Peroxisomal membrane protein 14 / Pex14 N-terminal domain / PEX5/PEX5L / Tetratricopeptide repeat / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Tetratricopeptide-like helical domain superfamily / Arc Repressor Mutant, subunit A / Winged helix-like DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Peroxisomal membrane protein PEX14 / Peroxisomal targeting signal 1 receptor
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR
AuthorsKooshapur, H. / Meyer, H.N. / Madl, T. / Sattler, M.
CitationJournal: J.Biol.Chem. / Year: 2014
Title: A Novel Pex14 Interacting Site of Human Pex5 is Critical for Matrix Protein Import Into Peroxisomes.
Authors: Neuhaus, A. / Kooshapur, H. / Wolf, J. / Meyer, H.N. / Madl, T. / Saidowsky, J. / Hambruch, E. / Lassam, A. / Jung, M. / Sattler, M. / Schliebs, W. / Erdmann, R.
History
DepositionJul 15, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 27, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 15, 2014Group: Database references
Revision 2.0May 15, 2024Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Other
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_spectrometer / pdbx_validate_close_contact
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_spectrometer.model / _pdbx_validate_close_contact.auth_atom_id_1

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: PEROXISOMAL MEMBRANE PROTEIN PEX14
B: PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR


Theoretical massNumber of molelcules
Total (without water)9,1612
Polymers9,1612
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / -
Representative

-
Components

#1: Protein PEROXISOMAL MEMBRANE PROTEIN PEX14 / PTS1 RECEPTOR-DOCKING PROTEIN / PEROXIN-14 / PEROXISOMAL MEMBRANE ANCHOR PROTEIN PEX14


Mass: 7453.446 Da / Num. of mol.: 1 / Fragment: RESIDUES 16-80
Source method: isolated from a genetically manipulated source
Details: RESIDUES 12-15 (GAMA) OF PEX14 ORIGINATE FROM THE EXPRESSION VECTOR
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O75381
#2: Protein/peptide PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR / PTS1 RECEPTOR / PTS1R / PTS1-BP / PEROXIN-5 / PEROXISOMAL C-TERMINAL TARGETING SIGNAL IMPORT ...PTS1 RECEPTOR / PTS1R / PTS1-BP / PEROXIN-5 / PEROXISOMAL C-TERMINAL TARGETING SIGNAL IMPORT RECEPTOR / PEROXISOME RECEPTOR 1 / PEX5


Mass: 1707.746 Da / Num. of mol.: 1 / Fragment: RESIDUES 57-71 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P50542

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: NONE

-
Sample preparation

Sample conditionspH: 6.5 / Temperature: 298.0 K

-
NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE5001
Bruker AVANCEBrukerAVANCE6002
Bruker AVANCEBrukerAVANCE9003

-
Processing

NMR softwareName: ARIA1.2/CNS / Developer: JP LINGE, SI O DONOGHUE / Classification: refinement
NMR ensembleConformers submitted total number: 10

+
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://pdbjlvh1.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