[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleSegmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 56, Issue 32, Page 9322-9325, Year 2017
Publish dateAug 1, 2017
AuthorsMiriam Sonntag / Pravin Kumar Ankush Jagtap / Bernd Simon / Marie-Sousai Appavou / Arie Geerlof / Ralf Stehle / Frank Gabel / Janosch Hennig / Michael Sattler /
PubMed AbstractMulti-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers ...Multi-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers undergo dynamic rearrangements upon binding to protein, DNA or RNA ligands. RNA binding proteins (RBPs) represent an important class of multi-domain proteins, which regulate gene expression by recognizing linear or structured RNA sequence motifs. Here, we employ segmental perdeuteration of the three RNA recognition motif (RRM) domains in the RBP TIA-1 using Sortase A mediated protein ligation. We show that domain-selective perdeuteration combined with contrast-matched small-angle neutron scattering (SANS), SAXS and computational modeling provides valuable information to precisely define relative domain arrangements. The approach is generally applicable to study conformational arrangements of individual domains in multi-domain proteins and changes induced by ligand binding.
External linksAngew Chem Int Ed Engl / PubMed:28636238
MethodsSAS (X-ray in house) / NMR (solution) / X-ray diffraction
Resolution2.97 Å
Structure data

SASDCC3: Nucleolysin TIA-1 isoform p40 in complex with U15 RNA
Method: SAXS/SANS

SASDCD3: Nucleolysin TIA-1 isoform p40 (LPQTG containing construct for sortase mediated protein ligation)
Method: SAXS/SANS

SASDCE3: Nucleolysin TIA-1 isoform p40 in complex with U15 RNA (LPQTG containing construct for sortase mediated protein ligation)
Method: SAXS/SANS

SASDCF3: Nucleolysin TIA-1 isoform p40 (TIA-1 wild type)
Method: SAXS/SANS

SASDCG3: Nucleolysin TIA-1 isoform p40 (LPATG containing construct for sortase mediated protein ligation)
Method: SAXS/SANS

SASDCH3: Nucleolysin TIA-1 isoform p40 in complex with U15 RNA (LPATG containing construct for sortase mediated protein ligation)
Method: SAXS/SANS

PDB-5o2v:
NMR structure of TIA-1 RRM1 domain
Method: SOLUTION NMR

PDB-5o3j:
Crystal structure of TIA-1 RRM2 in complex with RNA
Method: X-RAY DIFFRACTION / Resolution: 2.97 Å

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / RRM / TIA-1

+
About Yorodumi Papers

-
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 Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more