English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.

Jaremko, M., Jaremko, L., Nowakowski, M., Wojciechowski, M., Szczepanowski, R. H., Panecka, R., et al. (2013). NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme. Journal of Structural Biology, 185(1), 69-78. doi:10.1016/j.jsb.2013.10.020.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-7EBE-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E5CA-7
Genre: Journal Article

Files

show Files
hide Files
:
1936307.pdf (Publisher version), 4MB
Name:
1936307.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Jaremko, M.1, Author              
Jaremko, L.1, Author              
Nowakowski, M., Author
Wojciechowski, M., Author
Szczepanowski, R. H., Author
Panecka, R., Author
Zhukov, I., Author
Bochtler, M., Author
Ejchart, A., Author
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: Ubiquitin-activating enzyme E1; First catalytic cysteine half-domain (FCCH); Second catalytic cysteine half-domain (SCCH); NMR structure determination; N-15 nuclear magnetic relaxation; NMR study interactions in solution; Protein structure; Backbone dynamics
 Abstract: We report a high resolution NMR structure and N-15 relaxation studies of the first catalytic cysteine halfdomain (FCCH) of the mouse ubiquitin-activating enzyme El, together with interaction studies of FCCH and the other catalytic El subdomain - SCCH (second catalytic cysteine half-domain). In solution, mouse FCCH forms a well-defined six-stranded antiparallel 13-barrel structure, a common fold for many proteins with a variety of cellular functions. N-15 relaxation data reveal FCCH complex backbone dynamics and indicate which residues experience slow intramolecular motions. Some of these residues make contacts with the polar face of ubiquitin in the co-crystal structure of yeast E1 and ubiquitin. However, the titration of FCCH with ubiquitin does not show any visible chemical shift changes in the 2D H-1/N-15 HSQC spectra of the FCCH. The 2D H-1/N-15 HSQC experiments performed both for each catalytic half-domain individually and for their equimolar mixture in the milimolar concentration range display no detectable chemical shift perturbation, suggesting a lack of interaction between the two subdomains unless they are covalently linked via the adenylation domain. (C) 2013 Elsevier Inc. All rights reserved.

Details

show
hide
Language(s): eng - English
 Dates: 2013-11-06
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.jsb.2013.10.020
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Structural Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 185 (1) Sequence Number: - Start / End Page: 69 - 78 Identifier: -